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Human Metabolome Database Version 2.5

 

Showing metabocard for Protoporphyrin IX (HMDB00241)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-07 14:24:33
Accession Number HMDB00241
Secondary Accession Numbers Not Available
Common Name Protoporphyrin IX
Description Protoporphyrins are tetrapyrroles containing 4 methyl, 2 propionic and 2 vinyl side chains. Protopophyrin is produced by oxidation of the methylene bridge of protoporphyrinogen. Protoporphyrin IX is the only naturally occurring isomer; it is an intermediate in heme biosynthesis, combining with ferrous iron to form protoheme IX, the heme prosthetic group of hemoglobin. Protoporphyrin IX is created by the enzyme protoporphyrinogen oxidase. The enzyme ferrochelatase converts it into heme. Protoporphyrin IX naturally occurs in small amounts in feces. It is accumulated and excreted excessively in the feces in protoporphyria and variegate porphyria. Protoporphyrin IX is also responsible for the brown pigment (Ooporphyrin) of birds' eggs Protoporphyrin IX is used as a branch point in the biosynthetic pathway leading to Heme (by insertion of iron) and chlorophylls (by insertion of Mg and further side-chain transformation). Protoporphyrin IX can be used to treat liver disorders, mainly as the sodium salt. Shows anti-HIV activity.
Synonyms
  1. 3,3'-(3,7,12,17-tetramethyl-8,13-divinyl-21H,23H-porphine-2,18-diyl)-bis-propionate
  2. 3,3'-(3,7,12,17-tetramethyl-8,13-divinyl-21H,23H-porphine-2,18-diyl)-bis-propionic acid
  3. 3,3'-(3,7,12,17-tetramethyl-8,13-divinylporphine-2,18-diyl)di
  4. Kammerer's prophyrin
  5. Ooporphyrin
  6. Porphyrinogen IX
  7. Protoporphyrin
  8. Protoporphyrin IX
  9. ppIX
  10. protoporphyrin-"IX"
  11. protoporphyrin-IX
Chemical IUPAC Name 7,12-diethenyl-3,8,13,17-tetramethyl-21H,23H-Porphine-2,18-dipropanoic acid
Chemical Formula C34H34N4O4
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Heterocyclic molecules
Class
  • Porphyrins
Sub Class
  • Miscellaneous porphyrins
Family
  • Mammalian Metabolite
Species
  • carboxylic acid
  • alkene
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Porphyrin and chlorophyll metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 562.658
Monoisotopic Molecular Weight 562.257996
Isomeric SMILES CC1=C(CCC(O)=O)/C2=C/C3=N/C(=CC4=C(C)C(C=C)=C(N4)C=C4/N=C(/C=C1N2)C(C=C)=C/4C)/C(C)=C3CCC(O)=O
Canonical SMILES CC1=C(CCC(O)=O)C2=CC3=NC(=CC4=C(C)C(C=C)=C(N4)C=C4N=C(C=C1N2)C(C=C)=C4C)C(C)=C3CCC(O)=O
KEGG Compound ID C02191 Link Image
BioCyc ID PROTOPORPHYRIN_IX Link Image
BiGG ID 39293 Link Image
Wikipedia Link Protoporphyrin IX Link Image
NuGOwiki Link HMDB00241 Link Image
Metagene Link HMDB00241 Link Image
METLIN ID 4158 Link Image
PubChem Compound 4971 Link Image
PubChem Substance 11369318 Link Image
ChEBI ID 15430 Link Image
CAS Registry Number 553-12-8
InChI Identifier InChI=1/C34H34N4O4/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25/h7-8,13-16,35,38H,1-2,9-12H2,3-6H3,(H,39,40)(H,41,42)/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-
Synthesis Reference Games, David E.; Jackson, Anthony H.; Jackson, J. Richard; Belcher, Roderick V.; Smith, Sydney G. Biosynthesis of protoporphyrin-IX from coproporphyrinogen-III. Journal of the Chemical Society, Chemical Communications (1976), (6), 187-8.
Melting Point (Experimental) 300 oC
Experimental Water Solubility 0.169 mg/mL at 25 oC [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 0.0217 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 4.40 [Predicted by ALOGPS]; 2.9 [Predicted by PubChem via XLOGP]; 7.43 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1HBG Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • Mitochondria
  • Membrane (Predicted from LogP)
Biofluid Location
  • Blood
Tissue Location
Tissue References
Adipose Tissue —
Adrenal Medulla —
Bladder —
Erythrocyte —
Fibroblasts —
Gastrointestinal Tract —
Intestine —
Kidney —
Liver —
Lymphocyte —
Platelet —
Skin —
Spleen —
Stratum Corneum —
T-Lymphocyte —
Testes —
Thyroid Gland —
Urinary Bladder —
Concentrations (Normal)
Biofluid Blood
Value 0.66 +/- 0.18 uM
Age Adult:>18 yrs old
Sex Female
Patient information Women
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 0.53 +/- 0.13 uM
Age Adult:>18 yrs old
Sex Male
Patient information Men
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 1.09 +/- 0.57 uM
Age Newborn:0-30 days old
Sex Both
Patient information Newborns
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Porphyrin Metabolism SMP00024 Link Image map00860 Link Image
General References
  1. Messmann H, Knuchel R, Baumler W, Holstege A, Scholmerich J: Endoscopic fluorescence detection of dysplasia in patients with Barrett's esophagus, ulcerative colitis, or adenomatous polyps after 5-aminolevulinic acid-induced protoporphyrin IX sensitization. Gastrointest Endosc. 1999 Jan;49(1):97-101. [PubMed Link Image]
  2. Stankiewicz A, Lutz W, Krajewska B, Szulc B: [Plasma indicators of iron metabolism in persons occupationally exposed to organic solvents with normal and increased levels of protoporphyrin IX in erythrocytes] Pol Tyg Lek. 1986 Jul 7;41(27):851-4. [PubMed Link Image]
  3. Stankiewicz A: [Erythrocyte protoporphyrin IX in occupational exposure to asbestos] Med Pr. 1984;35(5):351-4. [PubMed Link Image]
  4. Sudworth CD, Stringer MR, Cruse-Sawyer JE, Brown SB: Fluorescence microspectroscopy technique for the study of intracellular protoporphyrin IX dynamics. Appl Spectrosc. 2003 Jun;57(6):682-8. [PubMed Link Image]
  5. Kufner G, Schlegel H, Jager R: A spectrophotometric micromethod for determining erythrocyte protoporphyrin-IX in whole blood or erythrocytes. Clin Chem Lab Med. 2005;43(2):183-91. [PubMed Link Image]
  6. Stankiewicz A: The concentration of protoporphyrin IX in workers occupationally exposed to lead. Mater Med Pol. 1989 Apr-Jun;21(2):100-2. [PubMed Link Image]
  7. Krieg RC, Fickweiler S, Wolfbeis OS, Knuechel R: Cell-type specific protoporphyrin IX metabolism in human bladder cancer in vitro. Photochem Photobiol. 2000 Aug;72(2):226-33. [PubMed Link Image]
  8. Bailey GG, Needham LL: Simultaneous quantification of erythrocyte zinc protoporphyrin and protoporphyrin IX by liquid chromatography. Clin Chem. 1986 Dec;32(12):2137-42. [PubMed Link Image]
  9. Chisolm J Jr, Brown DH: Micro-scale photofluorometric determination of "free erythrocyte pophyrin" (protoporphyrin IX). Clin Chem. 1975 Oct;21(11):1669-82. [PubMed Link Image]
  10. Casas A, Batlle AM, Butler AR, Robertson D, Brown EH, MacRobert A, Riley PA: Comparative effect of ALA derivatives on protoporphyrin IX production in human and rat skin organ cultures. Br J Cancer. 1999 Jul;80(10):1525-32. [PubMed Link Image]
  11. Smits T, Robles CA, van Erp PE, van de Kerkhof PC, Gerritsen MJ: Correlation between macroscopic fluorescence and protoporphyrin IX content in psoriasis and actinic keratosis following application of aminolevulinic acid. J Invest Dermatol. 2005 Oct;125(4):833-9. [PubMed Link Image]
  12. Bartosova J, Hrkal Z: Accumulation of protoporphyrin-IX (PpIX) in leukemic cell lines following induction by 5-aminolevulinic acid (ALA). Comp Biochem Physiol C Toxicol Pharmacol. 2000 Jul;126(3):245-52. [PubMed Link Image]
  13. Sakai T, Takeuchi Y, Ikeya Y, Araki T, Ushio K: [Automated HPLC method for determining zinc protoporphyrin IX and protoporphyrin IX in erythrocytes of workers exposed to lead] Sangyo Igaku. 1988 Nov;30(6):467-74. [PubMed Link Image]
  14. Stankiewicz A, Lutz W, Szeszko A: [Protoporphyrin IX level in erythrocytes of persons with alcoholic liver cirrhosis] Pol Tyg Lek. 1985 Jul 15;40(28):787-9. [PubMed Link Image]
  15. Star WM, Aalders MC, Sac A, Sterenborg HJ: Quantitative model calculation of the time-dependent protoporphyrin IX concentration in normal human epidermis after delivery of ALA by passive topical application or lontophoresis. Photochem Photobiol. 2002 Apr;75(4):424-32. [PubMed Link Image]
  16. von Beckerath M, Juzenas P, Ma LW, Iani V, Lofgren L, Moan J: The influence of UV exposure on 5-aminolevulinic acid-induced protoporphyrin IX production in skin. Photochem Photobiol. 2001 Dec;74(6):825-8. [PubMed Link Image]
  17. Gottsch JD, Graham CR Jr, Hairston RJ, Chen CH, Green WR, Stark WJ: Protoporphyrin IX photosensitization of corneal endothelium. Arch Ophthalmol. 1989 Oct;107(10):1497-500. [PubMed Link Image]
  18. Bissonnette R, Zeng H, McLean DI, Korbelik M, Lui H: Oral aminolevulinic acid induces protoporphyrin IX fluorescence in psoriatic plaques and peripheral blood cells. Photochem Photobiol. 2001 Aug;74(2):339-45. [PubMed Link Image]
  19. Rick K, Sroka R, Stepp H, Kriegmair M, Huber RM, Jacob K, Baumgartner R: Pharmacokinetics of 5-aminolevulinic acid-induced protoporphyrin IX in skin and blood. J Photochem Photobiol B. 1997 Oct;40(3):313-9. [PubMed Link Image]
  20. De Rosa FS, Marchetti JM, Thomazini JA, Tedesco AC, Bentley MV: A vehicle for photodynamic therapy of skin cancer: influence of dimethylsulphoxide on 5-aminolevulinic acid in vitro cutaneous permeation and in vivo protoporphyrin IX accumulation determined by confocal microscopy. J Control Release. 2000 Apr 3;65(3):359-66. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Coproporphyrinogen III oxidase, mitochondrial precursor
  2. Protoporphyrinogen oxidase
  3. Ferrochelatase, mitochondrial precursor
  4. cDNA FLJ76483, highly similar to Homo sapiens ferrochelatase
  5. Ferrochelatase (EC 4.99.1.1) (Fragment)
  6. Ferrochelatase (EC 4.99.1.1)
  7. Ferrochelatase (EC 4.99.1.1)
  8. CDNA FLJ35097 fis, clone PLACE6006222, highly similar to FERROCHELATASE (EC 4.99.1.1)
Enzyme 1 [top]
Enzyme 1 ID 5483
Enzyme 1 Name Coproporphyrinogen III oxidase, mitochondrial precursor
Enzyme 1 Synonyms
  1. Coproporphyrinogenase
  2. Coprogen oxidase
  3. COX
Enzyme 1 Gene Name CPOX
Enzyme 1 Protein Sequence >Coproporphyrinogen III oxidase, mitochondrial precursor 
MALQLGRLSSGPCWLVARGGCGGPRAWSQCGGGGLRAWSQRSAAGRVCRPPGPAGTEQSR
GLGHGSTSRGGPWVGTGLAAALAGLVGLATAAFGHVQRAEMLPKTSGTRATSLGRPEEEE
DELAHRCSSFMAPPVTDLGELRRRPGDMKTKMELLILETQAQVCQALAQVDGGANFSVDR
WERKEGGGGISCVLQDGCVFEKAGVSISVVHGNLSEEAAKQMRSRGKVLKTKDGKLPFCA
MGVSSVIHPKNPHAPTIHFNYRYFEVEEADGNKQWWFGGGCDLTPTYLNQEDAVHFHRTL
KEACDQHGPDLYPKFKKWCDDYFFIAHRGERRGIGGIFFDDLDSPSKEEVFRFVQSCARA
VVPSYIPLVKKHCDDSFTPQEKLWQQLRRGRYVEFNLLYDRGTKFGLFTPGSRIESILMS
LPLTARWEYMHSPSENSKEAEILEVLRHPRDWVR
Enzyme 1 Number of Residues 454
Enzyme 1 Molecular Weight 50152
Enzyme 1 Theoretical pI 8.33
Enzyme 1 GO Classification
Function
  • catalytic activity
  • coproporphyrinogen oxidase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
Process
  • cellular metabolism
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin biosynthesis
  • porphyrin metabolism
Component
—
Enzyme 1 General Function Coenzyme transport and metabolism
Enzyme 1 Specific Function Coproporphyrinogen-III + O(2) + 2 H(+) = protoporphyrinogen-IX + 2 CO(2) + 2 H(2)O
Enzyme 1 Pathways
Enzyme 1 Reactions
  • coproporphyrinogen-III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-15
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 825648 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P36551 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name HEM6_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >556 bp 
ATGGCCTTGCAGCTGGGCAGGCTGAGCTCGGGCCCCTGCTGGCTCGTGGCGCGGGGCGGC
TGCGGAGGGCCCCGCGCCTGGTCCCAGTGCGGCGGCGGAGGGCTCCGAGCCTGGTCCCAG
CGCAGCGCAGCCGGACGCGTCTGCCGGCCCCCTGGCCCGGCTGGCACGGAGCAGAGCCGC
GGGCTGGGGCACGGCTCGACGTCGAGAGGCGGCCCCTGGGTGGGGACAGGGCTGGCCGCG
GCGCTGGCGGGGTTGGTGGGGCTGGCCACCGCCGCCTTCGGGCATGTGCAGCGGGCGGAG
ATGTTGCCTAAGACCTCGGGGACGCGGGCCACTTCGCTGGGGAGGCCGGAGGAGGAGGAG
GATGAGCTGGCCCACCGCTGCAGCAGCTTCATGGCCCCGCCTGTGACCGACCTGGGCGAG
CTGCGAAGGAGGCCGGGCGACATGAAGACCAAGATGGAGCTGCTGATTCTGGAGACCCAG
GCCCAGGTGTGCCAGGCTCTGGCACAGGTAGACGGGGGCGCCAACTTTTCTGTGGACCGG
TGGGAGAGGAAGGAAG
Enzyme 1 GenBank Gene ID Z34531 Link Image
Enzyme 1 GeneCard ID CPOX Link Image
Enzyme 1 GenAtlas ID CPOX Link Image
Enzyme 1 HGNC ID HGNC:2321 Link Image
Enzyme 1 Chromosome Location 3
Enzyme 1 Locus 3q12
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Delfau-Larue MH, Martasek P, Grandchamp B: Coproporphyrinogen oxidase: gene organization and description of a mutation leading to exon 6 skipping. Hum Mol Genet. 1994 Aug;3(8):1325-30. [PubMed Link Image]
  2. Taketani S, Kohno H, Furukawa T, Yoshinaga T, Tokunaga R: Molecular cloning, sequencing and expression of cDNA encoding human coproporphyrinogen oxidase. Biochim Biophys Acta. 1994 Jan 4;1183(3):547-9. [PubMed Link Image]
  3. Martasek P, Camadro JM, Delfau-Larue MH, Dumas JB, Montagne JJ, de Verneuil H, Labbe P, Grandchamp B: Molecular cloning, sequencing, and functional expression of a cDNA encoding human coproporphyrinogen oxidase. Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):3024-8. [PubMed Link Image]
  4. Martasek P, Nordmann Y, Grandchamp B: Homozygous hereditary coproporphyria caused by an arginine to tryptophane substitution in coproporphyrinogen oxidase and common intragenic polymorphisms. Hum Mol Genet. 1994 Mar;3(3):477-80. [PubMed Link Image]
  5. Fujita H, Kondo M, Taketani S, Nomura N, Furuyama K, Akagi R, Nagai T, Terajima M, Galbraith RA, Sassa S: Characterization and expression of cDNA encoding coproporphyrinogen oxidase from a patient with hereditary coproporphyria. Hum Mol Genet. 1994 Oct;3(10):1807-10. [PubMed Link Image]
  6. Lamoril J, Martasek P, Deybach JC, Da Silva V, Grandchamp B, Nordmann Y: A molecular defect in coproporphyrinogen oxidase gene causing harderoporphyria, a variant form of hereditary coproporphyria. Hum Mol Genet. 1995 Feb;4(2):275-8. [PubMed Link Image]
  7. Daimon M, Gojyou E, Sugawara M, Yamatani K, Tominaga M, Sasaki H: A novel missense mutation in exon 4 of the human coproporphyrinogen oxidase gene in two patients with hereditary coproporphyria. Hum Genet. 1997 Feb;99(2):199-201. [PubMed Link Image]
  8. Lamoril J, Deybach JC, Puy H, Grandchamp B, Nordmann Y: Three novel mutations in the coproporphyrinogen oxidase gene. Hum Mutat. 1997;9(1):78-80. [PubMed Link Image]
  9. Schreiber WE, Zhang X, Senz J, Jamani A: Hereditary coproporphyria: exon screening by heteroduplex analysis detects three novel mutations in the coproporphyrinogen oxidase gene. Hum Mutat. 1997;10(3):196-200. [PubMed Link Image]
  10. Rosipal R, Lamoril J, Puy H, Da Silva V, Gouya L, De Rooij FW, Te Velde K, Nordmann Y, Martasek P, Deybach JC: Systematic analysis of coproporphyrinogen oxidase gene defects in hereditary coproporphyria and mutation update. Hum Mutat. 1999;13(1):44-53. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6309
Enzyme 2 Name Protoporphyrinogen oxidase
Enzyme 2 Synonyms
  1. PPO
Enzyme 2 Gene Name PPOX
Enzyme 2 Protein Sequence >Protoporphyrinogen oxidase 
MGRTVVVLGGGISGLAASYHLSRAPCPPKVVLVESSERLGGWIRSVRGPNGAIFELGPRG
IRPAGALGARTLLLVSELGLDSEVLPVRGDHPAAQNRFLYVGGALHALPTGLRGLLRPSP
PFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSI
RSCFPSLFQAEQTHRSILLGLLLGAGRTPQPDSALIRQALAERWSQWSLRGGLEMLPQAL
ETHLTSRGVSVLRGQPVCGLSLQAEGRWKVSLRDSSLEADHVISAIPASVLSELLPAEAA
PLARALSAITAVSVAVVNLQYQGAHLPVQGFGHLVPSSEDPGVLGIVYDSVAFPEQDGSP
PGLRVTVMLGGSWLQTLEASGCVLSQELFQQRAQEAAATQLGLKEMPSHCLVHLHKNCIP
QYTLGHWQKLESARQFLTAHRLPLTLAGASYEGVAVNDCIESGRQAAVSVLGTEPNS
Enzyme 2 Number of Residues 477
Enzyme 2 Molecular Weight 50766
Enzyme 2 Theoretical pI 8.24
Enzyme 2 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
  • protoporphyrinogen oxidase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin biosynthesis
  • porphyrin metabolism
Component
—
Enzyme 2 General Function Coenzyme transport and metabolism
Enzyme 2 Specific Function Catalyzes the 6-electron oxidation of protoporphyrinogen IX to form protoporphyrin IX
Enzyme 2 Pathways
Enzyme 2 Reactions
  • protoporphyrinogen-IX + 1.5 O2 = protoporphyrin-IX + 3 H2O
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 837328 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P50336 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PPOX_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1434 bp 
ATGGGCCGGACCGTGGTCGTGCTGGGCGGAGGCATCAGCGGCTTGGCCGCCAGTTACCAC
CTGAGCCGGGCCCCCTGCCCCCCTAAGGTGGTCCTAGTGGAGAGCAGTGAGCGTCTGGGA
GGCTGGATTCGCTCCGTTCGAGGCCCTAATGGTGCTATCTTTGAGCTTGGACCTCGGGGA
ATTAGGCCAGCGGGAGCCCTAGGGGCCCGGACCTTGCTCCTGGTTTCTGAGCTTGGCTTG
GATTCAGAAGTGCTGCCTGTCCGGGGAGACCACCCAGCTGCCCAGAACAGGTTCCTCTAC
GTGGGCGGTGCCCTGCATGCCCTACCCACTGGCCTCAGGGGGCTACTCCGCCCTTCACCC
CCCTTCTCCAAACCTCTGTTTTGGGCTGGGCTGAGGGAGCTGACCAAGCCCCGGGGCAAA
GAGCCTGATGAGACTGTGCACAGTTTTGCCCAGCGCCGCCTTGGACCTGAGGTGGCGTCT
CTAGCCATGGACAGTCTCTGCCGTGGAGTGTTTGCAGGCAACAGCCGTGAGCTCAGCATC
AGGTCCTGCTTTCCCAGTCTCTTCCAAGCTGAGCAAACCCATCGTTCCATATTACTGGGC
CTGCTGCTGGGGGCAGGGCGGACCCCACAGCCAGACTCAGCACTCATTCGCCAGGCCTTG
GCTGAGCGCTGGAGCCAGTGGTCACTTCGTGGAGGTCTAGAGATGTTGCCTCAGGCCCTT
GAAACCCACCTGACTAGTAGGGGGGTCAGTGTTCTCAGAGGCCAGCCGGTCTGTGGGCTC
AGCCTCCAGGCAGAAGGGCGCTGGAAGGTATCTCTAAGGGACAGCAGTCTGGAGGCTGAC
CACGTTATTAGTGCCATTCCAGCTTCAGTGCTCAGTGAGCTGCTCCCTGCTGAGGCTGCC
CCTCTGGCTCGTGCCCTGAGTGCCATCACTGCAGTGTCTGTAGCTGTGGTGAATCTGCAG
TACCAAGGAGCCCATCTGCCTGTCCAGGGATTTGGACATTTGGTGCCATCTTCAGAAGAT
CCAGGAGTCCTGGGAATCGTGTATGACTCAGTTGCTTTCCCTGAGCAGGACGGGAGCCCC
CCTGGCCTCAGAGTGACTGTGATGCTGGGAGGTTCCTGGTTACAGACACTGGAGGCTAGT
GGCTGTGTCTTATCTCAGGAGCTGTTTCAACAGCGGGCCCAGGAAGCAGCTGCTACACAA
TTAGGACTGAAGGAGATGCCGAGCCACTGCTTGGTCCATCTACACAAGAACTGCATTCCC
CAGTATACACTAGGTCACTGGCAAAAACTAGAGTCAGCTAGGCAATTCCTGACTGCTCAC
AGGTTGCCCCTGACTCTGGCTGGAGCCTCCTATGAGGGAGTTGCTGTTAATGACTGTATA
GAGAGTGGGCGCCAGGCAGCAGTCAGTGTCCTGGGCACAGAACCTAACAGCTGA
Enzyme 2 GenBank Gene ID U26446 Link Image
Enzyme 2 GeneCard ID PPOX Link Image
Enzyme 2 GenAtlas ID PPOX Link Image
Enzyme 2 HGNC ID HGNC:9280 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1q22
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Nishimura K, Taketani S, Inokuchi H: Cloning of a human cDNA for protoporphyrinogen oxidase by complementation in vivo of a hemG mutant of Escherichia coli. J Biol Chem. 1995 Apr 7;270(14):8076-80. [PubMed Link Image]
  2. Dailey TA, Dailey HA: Human protoporphyrinogen oxidase: expression, purification, and characterization of the cloned enzyme. Protein Sci. 1996 Jan;5(1):98-105. [PubMed Link Image]
  3. Deybach JC, Puy H, Robreau AM, Lamoril J, Da Silva V, Grandchamp B, Nordmann Y: Mutations in the protoporphyrinogen oxidase gene in patients with variegate porphyria. Hum Mol Genet. 1996 Mar;5(3):407-10. [PubMed Link Image]
  4. Meissner PN, Dailey TA, Hift RJ, Ziman M, Corrigall AV, Roberts AG, Meissner DM, Kirsch RE, Dailey HA: A R59W mutation in human protoporphyrinogen oxidase results in decreased enzyme activity and is prevalent in South Africans with variegate porphyria. Nat Genet. 1996 May;13(1):95-7. [PubMed Link Image]
  5. Frank J, Poh-Fitzpatrick MB, King LE Jr, Christiano AM: The genetic basis of "Scarsdale Gourmet Diet" variegate porphyria: a missense mutation in the protoporphyrinogen oxidase gene. Arch Dermatol Res. 1998 Aug;290(8):441-5. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6347
Enzyme 3 Name Ferrochelatase, mitochondrial precursor
Enzyme 3 Synonyms
  1. Protoheme ferro-lyase
  2. Heme synthetase
Enzyme 3 Gene Name FECH
Enzyme 3 Protein Sequence >Ferrochelatase, mitochondrial precursor 
MRSLGANMAAALRAAGVLLRDPLASSSWRVCQPWRWKSGAAAAAVTTETAQHAQGAKPQV
QPQKRKPKTGILMLNMGGPETLGDVHDFLLRLFLDRDLMTLPIQNKLAPFIAKRRTPKIQ
EQYRRIGGGSPIKIWTSKQGEGMVKLLDELSPNTAPHKYYIGFRYVHPLTEEAIEEMERD
GLERAIAFTQYPQYSCSTTGSSLNAIYRYYNQVGRKPTMKWSTIDRWPTHHLLIQCFADH
ILKELDHFPLEKRSEVVILFSAHSLPMSVVNRGDPYPQEVSATVQKVMERLEYCNPYRLV
WQSKVGPMPWLGPQTDESIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQVLAKEC
GVENIRRAESLNGNPLFSKALADLVHSHIQSNELCSKQLTLSCPLCVNPVCRETKSFFTS
QQL
Enzyme 3 Number of Residues 423
Enzyme 3 Molecular Weight 47863
Enzyme 3 Theoretical pI 8.91
Enzyme 3 GO Classification
Function
  • catalytic activity
  • ferrochelatase activity
  • lyase activity
Process
  • cellular metabolism
  • heme biosynthesis
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin biosynthesis
  • porphyrin metabolism
Component
—
Enzyme 3 General Function Coenzyme transport and metabolism
Enzyme 3 Specific Function Catalyzes the ferrous insertion into protoporphyrin IX
Enzyme 3 Pathways
Enzyme 3 Reactions
  • protoporphyrin + Fe2+ = protoheme + 2 H+
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-19
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 219656 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P22830 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name HEMH_HUMAN Link Image
Enzyme 3 PDB ID 1HRK Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1272 bp 
ATGCGTTCACTCGGCGCAAACATGGCTGCGGCCCTGCGCGCCGCGGGCGTCCTGCTCCGC
GATCCGCTGGCATCCAGCAGCTGGAGGGTCTGTCAGCCATGGAGGTGGAAGTCAGGTGCA
GCTGCAGCGGCCGTCACCACAGAAACAGCCCAGCATGCCCAGGGTGCAAAACCTCAAGTT
CAACCGCAGAAGAGGAAGCCGAAAACTGGAATATTAATGCTAAACATGGGAGGCCCTGAA
ACTCTTGGAGATGTTCACGACTTCCTTCTGAGACTCTTCTTGGACCAAGACCTCATGACA
CTTCCTATTCAGAATAAGCTGGCACCATTCATCGCCAAACGCCGAACCCCCAAGATTCAA
GAGCAGTACCGCAGGATTGGAGGCGGATCCCCCATCAAGATATGGACTTCCAAGCAGGGA
GAGGGCATGGTGAAGCTGCTGGATGAATTGTCCCCCAACACAGCCCCTCACAAATACTAT
ATTGGATTTCGGTACGTCCATCCTTTAACAGAAGAAGCAATTGAAGAGATGGAGAGAGAT
GGCCTAGAAAGGGCTATTGCTTTCACACAGTATCCACAGTACAGCTGCTCCACCACAGGC
AGCAGCTTAAATGCCATTTACAGATACTATAATCAAGTGGGACGGAAGCCCACGATGAAG
TGGAGCACTATTGACAGGTGGCCCACACATCACCTCCTCATCCAGTGCTTTGCAGATCAT
ATTCTAAAGGAACTGGACCATTTTCCACTTGAGAAGAGAAGCGAGGTGGTCATTCTGTTT
TCTGCTCACTCACTGCCGATGTCTGTGGTCAACAGAGGCGACCCATATCCTCAGGAGGTA
AGCGCCACTGTCCAAAAAGTCATGGAAAGGCTGGAGTACTGCAACCCCTACCGACTGGTG
TGGCAATCCAAGGTTGGTCCGATGCCCTGGTTGGGTCCTCAAACAGACGAATCTATCAAA
GGGCTTTGTGAGAGGGGGAGGAAGAATATCCTCTTGGTTCCGATAGCATTTACCAGTGAC
CATATTGAAACGCTGTATGAGCTGGACATCGAGTACTCTCAAGTTTTAGCCAAGGAGTGT
GGAGTTGAAAACATCAGAAGAGCTGAGTCTCTTAATGGAAATCCATTGTTCTCTAAGGCC
CTGGCCGACTTGGTGCATTCACACATCCAGTCAAACGAGCTGTGTTCCAAGCAGCTGACC
CTGAGCTGTCCGCTCTGTGTCAATCCTGTCTGCAGGGAGACTAAATCCTTCTTCACCAGC
CAGCAGCTGTGA
Enzyme 3 GenBank Gene ID D00726 Link Image
Enzyme 3 GeneCard ID FECH Link Image
Enzyme 3 GenAtlas ID FECH Link Image
Enzyme 3 HGNC ID HGNC:3647 Link Image
Enzyme 3 Chromosome Location 18
Enzyme 3 Locus 18q21.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Nakahashi Y, Taketani S, Okuda M, Inoue K, Tokunaga R: Molecular cloning and sequence analysis of cDNA encoding human ferrochelatase. Biochem Biophys Res Commun. 1990 Dec 14;173(2):748-55. [PubMed Link Image]
  2. Tugores A, Magness ST, Brenner DA: A single promoter directs both housekeeping and erythroid preferential expression of the human ferrochelatase gene. J Biol Chem. 1994 Dec 9;269(49):30789-97. [PubMed Link Image]
  3. Dailey HA, Sellers VM, Dailey TA: Mammalian ferrochelatase. Expression and characterization of normal and two human protoporphyric ferrochelatases. J Biol Chem. 1994 Jan 7;269(1):390-5. [PubMed Link Image]
  4. Crouse BR, Sellers VM, Finnegan MG, Dailey HA, Johnson MK: Site-directed mutagenesis and spectroscopic characterization of human ferrochelatase: identification of residues coordinating the [2Fe-2S] cluster. Biochemistry. 1996 Dec 17;35(50):16222-9. [PubMed Link Image]
  5. Sellers VM, Wang KF, Johnson MK, Dailey HA: Evidence that the fourth ligand to the [2Fe-2S] cluster in animal ferrochelatase is a cysteine. Characterization of the enzyme from Drosophila melanogaster. J Biol Chem. 1998 Aug 28;273(35):22311-6. [PubMed Link Image]
  6. Wu CK, Dailey HA, Rose JP, Burden A, Sellers VM, Wang BC: The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis. Nat Struct Biol. 2001 Feb;8(2):156-60. [PubMed Link Image]
  7. Cox TM: Erythropoietic protoporphyria. J Inherit Metab Dis. 1997 Jun;20(2):258-69. [PubMed Link Image]
  8. Lamoril J, Boulechfar S, de Verneuil H, Grandchamp B, Nordmann Y, Deybach JC: Human erythropoietic protoporphyria: two point mutations in the ferrochelatase gene. Biochem Biophys Res Commun. 1991 Dec 16;181(2):594-9. [PubMed Link Image]
  9. Brenner DA, Didier JM, Frasier F, Christensen SR, Evans GA, Dailey HA: A molecular defect in human protoporphyria. Am J Hum Genet. 1992 Jun;50(6):1203-10. [PubMed Link Image]
  10. Imoto S, Tanizawa Y, Sato Y, Kaku K, Oka Y: A novel mutation in the ferrochelatase gene associated with erythropoietic protoporphyria. Br J Haematol. 1996 Jul;94(1):191-7. [PubMed Link Image]
  11. Gouya L, Schneider-Yin X, Rufenacht U, Herrero C, Lecha M, Mascaro JM, Puy H, Deybach JC, Minder EI: Mutations in the ferrochelatase gene of four Spanish patients with erythropoietic protoporphyria. J Invest Dermatol. 1998 Sep;111(3):406-9. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 13086
Enzyme 4 Name cDNA FLJ76483, highly similar to Homo sapiens ferrochelatase
Enzyme 4 Synonyms
  1. protoporphyria
  2. FECH, mRNA
  3. Ferrochelatase
  4. Protoporphyria, isoform CRA_a
Enzyme 4 Gene Name FECH
Enzyme 4 Protein Sequence >cDNA FLJ76483, highly similar to Homo sapiens ferrochelatase 
MRSLGANMAAALRAAGVLLRDPLASSSWRVCQPWRWKSGAAAAAVTTETAQHAQGAKPQV
QPQKRKPKTGILMLNMGGPETLGDVHDFLLRLFLDRDLMTLPIQNKLAPFIAKRRTPKIQ
EQYRRIGGGSPIKIWTSKQGEGMVKLLDELSPNTAPHKYYIGFRYVHPLTEEAIEEMERD
GLERAIAFTQYPQYSCSTTGSSLNAIYRYYNQVGRKPTMKWSTIDRWPTHHLLIQCFADH
ILKELDHFPLEKRSEVVILFSAHSLPMSVVNRGDPYPQEVSATVQKVMERLEYCNPYRLV
WQSKVGPMPWLGPQTDESIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQVLAKEC
GVENIRRAESLNGNPLFSKALADLVHSHIQSNELCSKQLTLSCPLCVNPVCRETKSFFTS
QQL
Enzyme 4 Number of Residues 423
Enzyme 4 Molecular Weight 47863
Enzyme 4 Theoretical pI 8.91
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Coenzyme transport and metabolism
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function Not Available
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 158259335 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID A8KA72 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name A8KA72_HUMAN Link Image
Enzyme 4 PDB ID 1HRK Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID AK292937 Link Image
Enzyme 4 GeneCard ID A8KA72 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 14933
Enzyme 5 Name Ferrochelatase (EC 4.99.1.1) (Fragment)
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name Not Available
Enzyme 5 Protein Sequence >Ferrochelatase (EC 4.99.1.1) (Fragment) 
LGANMAAALRAAGVLLRDPLASSSWRVCQPWRWKSGAAAAAVTTETAQHAQGAKPQVQPQ
KRKPKTGILMLNMGGPETLGDVHDFLLRLFLDRDLMTLPIQNKLAPFIAKRRTPEIQEQY
RRIGGGSPIKIWTSKQGEGMVKLLDELSPNTAPHKYYIGFRYVHPLTEEAIEEMERDGLE
RAIAFTQYPQYSCSTTGSSLNAIYRYYNQVGRKPTMKWSTIDRWPTHHLLIQCFADHILK
ELDHFPLEKRSEVVILFSAHSLPMSVVNRGDPYPQEVSATVQKVMERLEYCNPYRLVWQS
KVGPMPWLGPQTDESIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQVLAKECGVE
NIRRAESLNGNPLFSKALADLVHSHIQSNELCSKQLTLSCPLCVNPVCRETKSFFTSQQL
Enzyme 5 Number of Residues 420
Enzyme 5 Molecular Weight 47489
Enzyme 5 Theoretical pI 8.53
Enzyme 5 GO Classification
Function
  • catalytic activity
  • ferrochelatase activity
  • lyase activity
Process
  • cellular metabolism
  • heme biosynthesis
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin biosynthesis
  • porphyrin metabolism
Component
—
Enzyme 5 General Function Coenzyme transport and metabolism
Enzyme 5 Specific Function Catalyzes the ferrous insertion into protoporphyrin IX
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions
  • protoheme + 2 H+ = protoporphyrin + Fe2+ [RN:R00310] ALL_REAC R00310
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 62897941 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q53FU1 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name Q53FU1_HUMAN Link Image
Enzyme 5 PDB ID 1HRK Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1263 bp 
CTCGGCGCAAACATGGCTGCGGCCCTGCGCGCCGCGGGCGTCCTGCTCCGCGATCCGCTG
GCATCCAGCAGCTGGAGGGTCTGTCAGCCATGGAGGTGGAAGTCAGGTGCAGCTGCAGCG
GCCGTCACCACAGAAACAGCCCAGCATGCCCAGGGTGCAAAACCTCAAGTTCAACCGCAG
AAGAGGAAGCCGAAAACTGGAATATTAATGCTAAACATGGGAGGCCCTGAAACTCTTGGA
GATGTTCACGACTTCCTTCTGAGACTCTTCTTGGACCGAGACCTCATGACACTTCCTATT
CAGAATAAGCTGGCACCATTCATCGCCAAACGCCGAACCCCCGAGATTCAAGAGCAGTAC
CGCAGGATTGGAGGCGGATCCCCCATCAAGATATGGACTTCCAAGCAGGGAGAGGGCATG
GTGAAGCTGCTGGATGAATTGTCCCCCAACACAGCCCCTCACAAATACTATATTGGATTT
CGGTACGTCCATCCTTTAACAGAAGAAGCAATTGAAGAGATGGAGAGAGATGGCCTAGAA
AGGGCTATTGCTTTCACACAGTATCCACAGTACAGCTGCTCCACCACAGGCAGCAGCTTA
AATGCCATTTACAGATACTATAATCAAGTGGGACGGAAGCCCACGATGAAGTGGAGCACT
ATTGACAGGTGGCCCACACATCACCTCCTCATCCAGTGCTTTGCAGATCATATTCTAAAG
GAACTGGACCATTTTCCACTTGAGAAGAGAAGCGAGGTGGTCATTCTGTTTTCTGCTCAC
TCACTGCCCATGTCTGTGGTCAACAGAGGCGACCCATATCCTCAGGAGGTAAGCGCCACT
GTCCAAAAAGTCATGGAAAGGCTGGAGTACTGCAACCCCTACCGACTGGTGTGGCAATCC
AAGGTTGGTCCAATGCCCTGGTTGGGTCCTCAAACAGACGAATCTATCAAAGGGCTTTGT
GAGAGGGGGAGGAAGAATATCCTCTTGGTTCCGATAGCATTTACCAGTGACCATATTGAA
ACGCTGTATGAGCTGGACATCGAGTACTCTCAAGTTTTAGCCAAGGAGTGTGGAGTTGAA
AACATCAGAAGAGCTGAGTCTCTTAATGGAAATCCATTGTTCTCTAAGGCCCTGGCCGAC
TTGGTGCATTCACACATCCAGTCAAACGAGCTGTGTTCCAAGCAGCTGACCCTGAGCTGT
CCGCTCTGTGTCAATCCTGTCTGCAGGGAGACTAAATCCTTCTTCACCAGCCAGCAGCTG
TGA
Enzyme 5 GenBank Gene ID AK223190 Link Image
Enzyme 5 GeneCard ID Q53FU1 Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID HGNC:3647 Link Image
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs Not Available
Enzyme 5 General References
  1. Maruyama K, Sugano S: Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene. 1994 Jan 28;138(1-2):171-4. [PubMed Link Image]
  2. Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S: Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. Gene. 1997 Oct 24;200(1-2):149-56. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 14936
Enzyme 6 Name Ferrochelatase (EC 4.99.1.1)
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name Not Available
Enzyme 6 Protein Sequence >Ferrochelatase (EC 4.99.1.1) 
MCSLGANMAAALRAAGVLLRDPLASSSWRVCQPWRWKSGAAAAAVTTETAQHAQGAKPQV
QPQKRKPKTGILMLNMGGPETLGDVHDFLLRLFLDRDLMTLPIQNKLAPFIAKRRTPKIQ
EQYRRIGGGSPIKIWTSKQGEGMVKLLDELSPNTAPHKYYIGFRYVHPLTEEAIEEMERD
GLERAIAFTQYPQYSCSTTGSSLNAIYRYYNQVGRKPTMKWSTIDRWPTHHLLIQCFADH
ILKELDHFPLERSEVVILFSAHSLPMSVVNRGDPYPQEVSATVQKVMERLEYCNPYRLVW
QSKVGPMPWLGPQTDESIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQVLAKECG
VENIRRAESLNGNPLFSKALADLVHSHIQSNELCSKQLTLSCPLCVNPVCRETKSFFTSQ
QL
Enzyme 6 Number of Residues 422
Enzyme 6 Molecular Weight 47682
Enzyme 6 Theoretical pI 8.59
Enzyme 6 GO Classification
Function
  • catalytic activity
  • ferrochelatase activity
  • lyase activity
Process
  • cellular metabolism
  • heme biosynthesis
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin biosynthesis
  • porphyrin metabolism
Component
—
Enzyme 6 General Function Coenzyme transport and metabolism
Enzyme 6 Specific Function Catalyzes the ferrous insertion into protoporphyrin IX
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions
  • protoheme + 2 H+ = protoporphyrin + Fe2+ [RN:R00310] ALL_REAC R00310
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 54696780 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q5TZY0 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name Q5TZY0_HUMAN Link Image
Enzyme 6 PDB ID 1HRK Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1269 bp 
ATGTGTTCACTCGGCGCAAACATGGCTGCGGCCCTGCGCGCCGCGGGCGTCCTGCTCCGC
GATCCGCTGGCATCCAGCAGCTGGAGGGTCTGTCAGCCATGGAGGTGGAAGTCAGGTGCA
GCTGCAGCGGCCGTCACCACAGAAACAGCCCAGCATGCCCAGGGTGCAAAACCTCAAGTT
CAACCGCAGAAGAGGAAGCCGAAAACTGGAATATTAATGCTAAACATGGGAGGCCCTGAA
ACTCTTGGAGATGTTCACGACTTCCTTCTGAGACTCTTCTTGGACCGAGACCTCATGACA
CTTCCTATTCAGAATAAGCTGGCACCATTCATCGCCAAACGCCGAACCCCCAAGATTCAA
GAGCAGTACCGCAGGATTGGAGGCGGATCCCCCATCAAGATATGGACTTCCAAGCAGGGA
GAGGGCATGGTGAAGCTGCTGGATGAATTGTCCCCCAACACAGCCCCTCACAAATACTAT
ATTGGATTTCGGTACGTCCATCCTTTAACAGAAGAAGCAATTGAAGAGATGGAGAGAGAT
GGCCTAGAAAGGGCTATTGCTTTCACACAGTATCCACAGTACAGCTGCTCCACCACAGGC
AGCAGCTTAAATGCCATTTACAGATACTATAATCAAGTGGGACGGAAGCCCACGATGAAG
TGGAGCACTATTGACAGGTGGCCCACACATCACCTCCTCATCCAGTGCTTTGCAGATCAT
ATTCTAAAGGAACTGGACCATTTTCCACTTGAGAGAAGCGAGGTGGTCATTCTGTTTTCT
GCTCACTCACTGCCGATGTCTGTGGTCAACAGAGGCGACCCATATCCTCAGGAGGTAAGC
GCCACTGTCCAAAAAGTCATGGAAAGGCTGGAGTACTGCAACCCCTACCGACTGGTGTGG
CAATCCAAGGTTGGTCCGATGCCCTGGTTGGGTCCTCAAACAGACGAATCTATCAAAGGG
CTTTGTGAGAGGGGGAGGAAGAATATCCTCTTGGTTCCGATAGCATTTACCAGTGACCAT
ATTGAAACGCTGTATGAGCTGGACATCGAGTACTCTCAAGTTTTAGCCAAGGAGTGTGGA
GTTGAAAACATCAGAAGAGCTGAGTCTCTTAATGGAAATCCATTGTTCTCTAAGGCCCTG
GCCGACTTGGTGCATTCACACATCCAGTCAAACGAGCTGTGTTCCAAGCAGCTGACCCTG
AGCTGTCCGCTCTGTGTCAATCCTGTCTGCAGGGAGACTAAATCCTTCTTCACCAGCCAG
CAGCTGTAG
Enzyme 6 GenBank Gene ID BT019959 Link Image
Enzyme 6 GeneCard ID Q5TZY0 Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID HGNC:3647 Link Image
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs Not Available
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 14937
Enzyme 7 Name Ferrochelatase (EC 4.99.1.1)
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name DKFZp686P18130
Enzyme 7 Protein Sequence >Ferrochelatase (EC 4.99.1.1) 
MAAALRAAGVLLRDPLASSSWRVCQPWRWKSGAAAAAVTTETAQHAQGAKPQVQPQKRKP
KTGILMLNMGGPETLGDVHDFLLRLFLDRDLMTLPIQNKLAPFIAKRRTPKIQEQYRRIG
GGSPIKIWTSKQGEGMVKLLDELSPNTAPHKYYIGFRYVHPLTEEAIEEMERDGLERAIA
FTQYPQYSCSTTGSSLNAIYRYYNQVGRKPTMKWSTIDRWPTHHLLIQCFADHILKELDH
FPLEKRSEVVILFSAHSLPMSVVNRGDPYPQEVSATVQKVMERLEYCNPYRLVWQSKVGP
MPWLGPQTDESIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQVLAKECGVENIRR
AESLNGNPLFSKALADLVHSHIQSNELCSKQLTLSCPLCVNPVCRETKSFFTSQQL
Enzyme 7 Number of Residues 416
Enzyme 7 Molecular Weight 47133
Enzyme 7 Theoretical pI 8.78
Enzyme 7 GO Classification
Function
  • catalytic activity
  • ferrochelatase activity
  • lyase activity
Process
  • cellular metabolism
  • heme biosynthesis
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin biosynthesis
  • porphyrin metabolism
Component
—
Enzyme 7 General Function Coenzyme transport and metabolism
Enzyme 7 Specific Function Catalyzes the ferrous insertion into protoporphyrin IX
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions
  • protoheme + 2 H+ = protoporphyrin + Fe2+ [RN:R00310] ALL_REAC R00310
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 33096717 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q7KZA3 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name Q7KZA3_HUMAN Link Image
Enzyme 7 PDB ID 1HRK Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1251 bp 
ATGGCTGCGGCCCTGCGCGCCGCGGGCGTCCTGCTCCGCGATCCGCTGGCATCCAGCAGC
TGGAGGGTCTGTCAGCCATGGAGGTGGAAGTCAGGTGCAGCTGCAGCGGCCGTCACCACA
GAAACAGCCCAGCATGCCCAGGGTGCAAAACCTCAAGTTCAACCGCAGAAGAGGAAGCCG
AAAACTGGAATATTAATGCTAAACATGGGAGGCCCTGAAACTCTTGGAGATGTTCACGAC
TTCCTTCTGAGACTCTTCTTGGACCGAGACCTCATGACACTTCCTATTCAGAATAAGCTG
GCACCATTCATCGCCAAACGCCGAACCCCCAAGATTCAAGAGCAGTACCGCAGGATTGGA
GGCGGATCCCCCATCAAGATATGGACTTCCAAGCAGGGAGAGGGCATGGTAAAGCTGCTG
GATGAATTGTCCCCCAACACAGCCCCTCACAAATACTATATTGGATTTCGGTACGTCCAT
CCTTTAACAGAAGAAGCAATTGAAGAGATGGAGAGAGATGGCCTAGAAAGGGCTATTGCT
TTCACACAGTATCCACAGTACAGCTGCTCCACCACAGGCAGCAGCTTAAATGCCATTTAC
AGATACTATAATCAAGTGGGACGGAAGCCCACGATGAAGTGGAGCACTATTGACAGGTGG
CCCACACATCACCTCCTCATCCAGTGCTTTGCAGATCATATTCTAAAGGAACTGGACCAT
TTTCCACTTGAGAAGAGAAGCGAGGTGGTCATTCTGTTTTCTGCTCACTCACTGCCGATG
TCTGTGGTCAACAGAGGCGACCCATATCCTCAGGAGGTAAGCGCCACTGTCCAAAAAGTC
ATGGAAAGGCTGGAGTACTGCAACCCCTACCGACTGGTGTGGCAATCCAAGGTTGGTCCG
ATGCCCTGGTTGGGTCCTCAAACAGACGAATCTATCAAAGGGCTTTGTGAGAGGGGGAGG
AAGAATATCCTCTTGGTTCCGATAGCATTTACCAGTGACCATATTGAAACGCTGTATGAG
CTGGACATCGAGTACTCTCAAGTTTTAGCCAAGGAGTGTGGAGTTGAAAACATCAGAAGA
GCTGAGTCTCTTAATGGAAATCCATTGTTCTCTAAGGCCCTGGCCGACTTGGTGCATTCA
CACATCCAGTCAAACGAGCTGTGTTCCAAGCAGCTGACCCTGAGCTGTCCGCTCTGTGTC
AATCCTGTCTGCAGGGAGACTAAATCCTTCTTCACCAGCCAGCAGCTGTGA
Enzyme 7 GenBank Gene ID BX571744 Link Image
Enzyme 7 GeneCard ID Q7KZA3 Link Image
Enzyme 7 GenAtlas ID DKFZp686P18130 Link Image
Enzyme 7 HGNC ID HGNC:3647 Link Image
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References Not Available
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 14938
Enzyme 8 Name CDNA FLJ35097 fis, clone PLACE6006222, highly similar to FERROCHELATASE (EC 4.99.1.1)
Enzyme 8 Synonyms Not Available
Enzyme 8 Gene Name Not Available
Enzyme 8 Protein Sequence >CDNA FLJ35097 fis, clone PLACE6006222, highly similar to FERROCHELATASE (EC 4.99.1.1) 
MRSLGANMAAALRAAGVLLRDPLASSSWRVCQPWRWKSGAAAAAVTTETAQHAQGAKPQV
QPQKRYESNIRKPKTGILMLNMGGPETLGDVHDFLLRLFLDRDLMTLPIQNKLAPFIAKR
RTPKIQEQYRRIGGGSPIKIWTSKQGEGMVKLLDELSPNTAPHKYYIGFRYVHPLTEEAI
EEMERDGLERAIAFTQYPQYSCSTTGSSLNAIYRYYNQVGRKPTMKWSTIDRWSTHHLLI
QCFADHILKELDHFPLEKRSEVVILFSAHSLPMSVVNRGDPYPQEVSATVQKVMERLEYC
NPYRLVWQSKVGPMPWLGPQTDESIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQ
VLAKECGVENIRRAESLNGNPLFSKALADLVHSHIQSNELCSKQLTLSCPLCVNPVCRET
KSFFTSQQL
Enzyme 8 Number of Residues 429
Enzyme 8 Molecular Weight 48616
Enzyme 8 Theoretical pI 8.90
Enzyme 8 GO Classification
Function
  • catalytic activity
  • ferrochelatase activity
  • lyase activity
Process
  • cellular metabolism
  • heme biosynthesis
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin biosynthesis
  • porphyrin metabolism
Component
—
Enzyme 8 General Function Coenzyme transport and metabolism
Enzyme 8 Specific Function Catalyzes the ferrous insertion into protoporphyrin IX
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions
  • protoheme + 2 H+ = protoporphyrin + Fe2+ [RN:R00310] ALL_REAC R00310
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 21751005 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q8NAN0 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name Q8NAN0_HUMAN Link Image
Enzyme 8 PDB ID 1HRK Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1290 bp 
ATGCGTTCACTCGGCGCAAACATGGCTGCGGCCCTGCGCGCCGCGGGCGTCCTGCTCCGC
GATCCGCTGGCATCCAGCAGCTGGAGGGTCTGTCAGCCATGGAGGTGGAAGTCAGGTGCA
GCTGCAGCGGCCGTCACCACAGAAACAGCCCAGCATGCCCAGGGTGCAAAACCTCAAGTT
CAACCGCAGAAGAGGTATGAGTCTAACATCAGGAAGCCGAAAACTGGAATATTAATGCTA
AACATGGGAGGCCCTGAAACTCTTGGAGATGTTCACGACTTCCTTCTGAGACTCTTCTTG
GACCGAGACCTCATGACACTTCCTATTCAGAATAAGCTGGCACCATTCATCGCCAAACGC
CGAACCCCCAAGATTCAAGAGCAGTACCGCAGGATTGGAGGCGGATCCCCCATCAAGATA
TGGACTTCCAAGCAGGGAGAGGGCATGGTGAAGCTGCTGGATGAATTGTCCCCCAACACA
GCCCCTCACAAATACTATATTGGATTTCGGTACGTCCATCCTTTAACAGAAGAAGCAATT
GAAGAGATGGAGAGAGATGGCCTAGAAAGGGCTATTGCTTTCACACAGTATCCACAGTAC
AGCTGCTCCACCACAGGCAGCAGCTTAAATGCCATTTACAGATACTATAATCAAGTGGGA
CGGAAGCCCACGATGAAGTGGAGCACTATTGACAGGTGGTCCACACATCACCTCCTCATC
CAGTGCTTTGCAGATCATATTCTAAAGGAACTGGACCATTTTCCACTTGAGAAGAGAAGC
GAGGTGGTCATTCTGTTTTCTGCTCACTCACTGCCCATGTCTGTGGTCAACAGAGGCGAC
CCATATCCTCAGGAGGTAAGCGCCACTGTCCAAAAAGTCATGGAAAGGCTGGAGTACTGC
AACCCCTACCGACTGGTGTGGCAATCCAAGGTTGGTCCGATGCCCTGGTTGGGTCCTCAA
ACAGACGAATCTATCAAAGGGCTTTGTGAGAGGGGGAGGAAGAATATCCTCTTGGTTCCG
ATAGCATTTACCAGTGACCATATTGAAACGCTGTATGAGCTGGACATCGAGTACTCTCAA
GTTTTAGCCAAGGAGTGTGGAGTTGAAAACATCAGAAGAGCTGAGTCTCTTAATGGAAAT
CCATTGTTCTCTAAGGCCCTGGCCGACTTGGTGCATTCACACATCCAGTCAAACGAGCTG
TGTTCCAAGCAGCTGACCCTGAGCTGTCCGCTCTGTGTCAATCCTGTCTGCAGGGAGACT
AAATCCTTCTTCACCAGCCAGCAGCTGTGA
Enzyme 8 GenBank Gene ID AK092416 Link Image
Enzyme 8 GeneCard ID Q8NAN0 Link Image
Enzyme 8 GenAtlas ID Not Available
Enzyme 8 HGNC ID HGNC:3647 Link Image
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
Enzyme 8 SNPs Not Available
Enzyme 8 General References Not Available
Enzyme 8 Metabolite References Not Available