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Human Metabolome Database Version 2.5

 

Showing metabocard for Uroporphyrin III (HMDB00916)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-08-12 15:16:44
Accession Number HMDB00916
Secondary Accession Numbers Not Available
Common Name Uroporphyrin III
Description Uroporphyrin is the porphyrin produced by oxidation of the methylene bridges in uroporphyrinogen. They have four acetic acid and four propionic acid side chains attached to the pyrrole rings. Uroporphyrinogen I and III are formed from polypyrryl methane in the presence of uroporphyrinogen III cosynthetase and uroporphyrin I synthetase, respectively. They can yield uroporphyrins by autooxidation or coproporphyrinogens by decarboxylation. Excessive amounts of uroporphyrin I are excreted in congenital erythropoietic porphyria, and both types I and III are excreted in porphyria cutanea tarda. Uroporphyrin I and III are the most common isomers.
Synonyms
  1. 3,8,13,17-tetrakis(carboxymethyl)porphyrin-2,7,12,18-tetrapropanoate
  2. 3,8,13,17-tetrakis(carboxymethyl)porphyrin-2,7,12,18-tetrapropanoic acid
  3. 3,8,13,17-tetramethyl-2,7,12,18-Porphinetetrapropionate
  4. 3,8,13,17-tetramethyl-2,7,12,18-Porphinetetrapropionic acid
  5. Coproporphyrin III
  6. Uroporphyrin III
Chemical IUPAC Name 3,8,13,17-tetrakis(carboxymethyl)porphyrin-2,7,12,18-tetrapropanoic acid
Chemical Formula C40H38N4O16
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Heterocyclic molecules
Class
  • Porphyrins
Sub Class
  • Uroporphyrins
Family
  • Microbial Metabolite
Species
  • carboxylic acid
  • aromatic compound
  • heterocyclic compound
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 830.747
Monoisotopic Molecular Weight 830.228271
Isomeric SMILES OC(=O)CCC1=C2NC(/C=C3N=C(C=C4NC(=CC5=NC(=C/2)C(CCC(O)=O)=C5CC(O)=O)/C(CC(O)=O)=C4CCC(O)=O)C(CC(O)=O)=C3CCC(O)=O)=C1CC(O)=O
Canonical SMILES OC(=O)CCC1=C2NC(C=C3N=C(C=C4NC(=CC5=NC(=C2)C(CCC(O)=O)=C5CC(O)=O)C(CC(O)=O)=C4CCC(O)=O)C(CC(O)=O)=C3CCC(O)=O)=C1CC(O)=O
KEGG Compound ID C02469 Link Image
BioCyc ID UROPORPHYRIN_III Link Image
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB00916 Link Image
Metagene Link HMDB00916 Link Image
METLIN ID 5870 Link Image
PubChem Compound Not Available
PubChem Substance 5484 Link Image
ChEBI ID 15436 Link Image
CAS Registry Number 18273-06-8
InChI Identifier InChI=1/C40H38N4O16/c45-33(46)5-1-17-21(9-37(53)54)29-14-27-19(3-7-35(49)50)22(10-38(55)56)30(43-27)15-28-20(4-8-36(51)52)24(12-40(59)60)32(44-28)16-31-23(11-39(57)58)18(2-6-34(47)48)26(42-31)13-25(17)41-29/h13-16,41,44H,1-12H2,(H,45,46)(H,47,48)(H,49,50)(H,51,52)(H,53,54)(H,55,56)(H,57,58)(H,59,60)/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-
Synthesis Reference Kajiwara, Masahiro; Mizutani, Minoru; Kojima, Ichiro. Manufacture of uroporphyrin III with Arthrobacter. Jpn. Kokai Tokkyo Koho (1993), 7 pp.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.0366 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -8
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 0.75 [Predicted by ALOGPS]; -3.8 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1R3T Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • mitochondria
Biofluid Location
  • Urine
Tissue Location
Tissue References
Liver —
Concentrations (Normal) Not Available
Concentrations (Abnormal)
Biofluid Urine
Value 0.00005 (0.00005-0.0007) umol/mmol creatinine
Age Newborn:0-30 days old
Sex Both
Comments Not Available
References
  • Ozalla D, Herrero C, Ribas-Fito N, To-Figueras J, Toll A, Sala M, Grimalt J, Basagana X, Lecha M, Sunyer J: Evaluation of urinary porphyrin excretion in neonates born to mothers exposed to airborne hexachlorobenzene. Environ Health Perspect. 2002 Feb;110(2):205-9. [PubMed Link Image]
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. Tsai SF, Bishop DF, Desnick RJ: Purification and properties of uroporphyrinogen III synthase from human erythrocytes. J Biol Chem. 1987 Jan 25;262(3):1268-73. [PubMed Link Image]
  2. Bozek P, Hutta M, Hrivnakova B: Rapid analysis of porphyrins at low ng/l and microg/l levels in human urine by a gradient liquid chromatography method using octadecylsilica monolithic columns. J Chromatogr A. 2005 Aug 19;1084(1-2):24-32. [PubMed Link Image]
  3. Ohdoi C, Nyhan WL, Kuhara T: Chemical diagnosis of Lesch-Nyhan syndrome using gas chromatography-mass spectrometry detection. J Chromatogr B Analyt Technol Biomed Life Sci. 2003 Jul 15;792(1):123-30. [PubMed Link Image]
  4. Luo J, Lim CK: Isolation and characterization of new porphyrin metabolites in human porphyria cutanea tarda and in rats treated with hexachlorobenzene by HPTLC, HPLC and liquid secondary ion mass spectrometry. Biomed Chromatogr. 1995 May-Jun;9(3):113-22. [PubMed Link Image]
  5. Schonning C, Leeming R, Stenstrom TA: Faecal contamination of source-separated human urine based on the content of faecal sterols. Water Res. 2002 Apr;36(8):1965-72. [PubMed Link Image]
  6. Hernandez-Zavala A, Del Razo LM, Garcia-Vargas GG, Aguilar C, Borja VH, Albores A, Cebrian ME: Altered activity of heme biosynthesis pathway enzymes in individuals chronically exposed to arsenic in Mexico. Arch Toxicol. 1999 Mar;73(2):90-5. [PubMed Link Image]
  7. Salen G, Berginer V, Shore V, Horak I, Horak E, Tint GS, Shefer S: Increased concentrations of cholestanol and apolipoprotein B in the cerebrospinal fluid of patients with cerebrotendinous xanthomatosis. Effect of chenodeoxycholic acid. N Engl J Med. 1987 May 14;316(20):1233-8. [PubMed Link Image]
  8. To-Figueras J, Ozalla D, Mateu CH: Long-standing changes in the urinary profile of porphyrin isomers after clinical remission of porphyria cutanea tarda. Ann Clin Lab Sci. 2003 Summer;33(3):251-6. [PubMed Link Image]
Metabolic Enzymes
  1. Porphyrin biosynthesis protein includes: uroporphyrinogen-III methyltransferase and uroporphyrinogen-III synthase] (EC 2.1.1.107) (EC 4.2.1.75)
  2. Uroporphyrinogen III methylase
  3. Uroporphyrinogen-III methyltransferase/synthase (EC 4.2.1.75) (EC 2.1.1.107)
  4. Uroporphyrinogen-III methyltransferase/synthase (EC 4.2.1.75) (EC 2.1.1.107)
  5. Siroheme synthase
  6. Putative uroporphyrinogen-III C-methyltransferase
  7. Fused siroheme synthase 1,3-dimethyluroporphyriongen III dehydrogenase and siroheme ferrochelatase
Enzyme 1 [top]
Enzyme 1 ID 15856
Enzyme 1 Name Porphyrin biosynthesis protein includes: uroporphyrinogen-III methyltransferase and uroporphyrinogen-III synthase] (EC 2.1.1.107) (EC 4.2.1.75)
Enzyme 1 Synonyms Not Available
Enzyme 1 Gene Name hemD
Enzyme 1 Protein Sequence >Porphyrin biosynthesis protein includes: uroporphyrinogen-III methyltransferase and uroporphyrinogen-III synthase] (EC 2.1.1.107) (EC 4.2.1.75) 
MRIMKGKVYLVGAGPGDYKLMTLKGLECIRKSDVIVYDRLANSSYLREAKPDCELIYVGK
ASSNHILPQEDINRIIAEKAKEGKIVTRLKGGDPYVFGRGGEEAETLVDEGIEFEVVPGI
TSAIGGLCYAGIPITHRDHASSFHVITGHLKGDDSGELNWNALANNKGTLVFLMGISNLE
KISENLMKEGKDKDTPVALISWATRYNQRVVTSTLENVYETAIKEEVKPPTLIVVGSVVG
LREKLNFFESKPLFGKSIAVTRSRNQNSVLVEKIMDLGGNPIEIPTIKVEKIQNNINLEN
EIKNINKYNYLILTSKNAVEIFFEKIYEMNFDLRILSNLKVCAIGSATSNELKKRGIIAD
IVPKKFVAESLYEELAPILNDDDNILIPRAENARDYLVDKLKAICEVTEVHIYRTVIDEE
KKGEILDILNSNDIDYITFTSSSTVNNLVEIIGKENIKILEKIKTLSIGPITTETINSLG
IKLYKESATSTIDSLVDLIIKN
Enzyme 1 Number of Residues 502
Enzyme 1 Molecular Weight 55826
Enzyme 1 Theoretical pI 5.47
Enzyme 1 GO Classification
Function
  • C-methyltransferase activity
  • carbon-oxygen lyase activity
  • catalytic activity
  • hydro-lyase activity
  • lyase activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • uroporphyrin-III C-methyltransferase activity
  • uroporphyrinogen-III synthase activity
Process
  • cellular metabolism
  • cobalamin biosynthesis
  • heme biosynthesis
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin biosynthesis
  • porphyrin metabolism
Component
—
Enzyme 1 General Function Coenzyme transport and metabolism
Enzyme 1 Specific Function Not Available
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions
  • hydroxymethylbilane = uroporphyrinogen III + H2O [RN:R03165] ALL_REAC R03165
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein Not Available
Enzyme 1 UniProtKB/Swiss-Prot ID Q180R8 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name Q180R8_CLOD6 Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence Not Available
Enzyme 1 GenBank Gene ID AM180355 Link Image
Enzyme 1 GeneCard ID Not Available
Enzyme 1 GenAtlas ID Not Available
Enzyme 1 HGNC ID Not Available
Enzyme 1 Chromosome Location Not Available
Enzyme 1 Locus Not Available
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References Not Available
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 15857
Enzyme 2 Name Uroporphyrinogen III methylase
Enzyme 2 Synonyms Not Available
Enzyme 2 Gene Name hemX
Enzyme 2 Protein Sequence >Uroporphyrinogen III methylase 
MSKKAYIIGAGPGDEELLTLKAINALQKCTAVLYDRLVGNNILNYLNDDCEIYYCGKEPG
CHYKTQEEINESIVELAKKGHVVGRVKGGDPYVFGRGGEEVLALVEENIPFEVIPGVTSP
ISVLNYAGIPITHRGLAQSFHIVTGMSARTLNVNWEALSKENGTLVFMMGLSNLETIVEK
LLENGKDIETPCGVVMRGTTSKQRKVIGTLENICKKVREAKLESPCIIVVGDVVSLNEKL
SWYEKLPLFGANICLTRSKEQSKEIKWKLKELGAEVTEINSIKIKKTAENLDEYINTLEK
YDHIVFTSVNAVNVFFDYLVKNRVDIRKIKADFAVLGKATKKALISRGIVPSIMAHSFTA
EGLFEVLKDNIKEGEEVLIPCSSLSREYLFDNLASLGAKCHRVNIYDTVCGDVKNPRAFK
EVDMVLYTSPSTVKNMIDMIGLEALKEKVSIAIGPITLKALNESGIEGKMCKTHCGDGFL
SEIEGIWQEVKK
Enzyme 2 Number of Residues 492
Enzyme 2 Molecular Weight 54450
Enzyme 2 Theoretical pI 6.70
Enzyme 2 GO Classification
Function
  • C-methyltransferase activity
  • carbon-oxygen lyase activity
  • catalytic activity
  • hydro-lyase activity
  • lyase activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • uroporphyrin-III C-methyltransferase activity
  • uroporphyrinogen-III synthase activity
Process
  • cellular metabolism
  • cobalamin biosynthesis
  • heme biosynthesis
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin biosynthesis
  • porphyrin metabolism
Component
—
Enzyme 2 General Function Coenzyme transport and metabolism
Enzyme 2 Specific Function Not Available
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein Not Available
Enzyme 2 UniProtKB/Swiss-Prot ID Q8XKG5 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name Q8XKG5_CLOPE Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence Not Available
Enzyme 2 GenBank Gene ID BA000016 Link Image
Enzyme 2 GeneCard ID Not Available
Enzyme 2 GenAtlas ID Not Available
Enzyme 2 HGNC ID Not Available
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Shimizu T, Ohtani K, Hirakawa H, Ohshima K, Yamashita A, Shiba T, Ogasawara N, Hattori M, Kuhara S, Hayashi H: Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater. Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):996-1001. Epub 2002 Jan 15. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 15858
Enzyme 3 Name Uroporphyrinogen-III methyltransferase/synthase (EC 4.2.1.75) (EC 2.1.1.107)
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name hemD
Enzyme 3 Protein Sequence >Uroporphyrinogen-III methyltransferase/synthase (EC 4.2.1.75) (EC 2.1.1.107) 
MSKKAYIIGAGPGDEELLTLKAINALQKCTAVLYDRLVGNNILNYLNDDCEIYYCGKEPG
CHYKTQEEINESIVELAKKGHVVGRVKGGDPYVFGRGGEEVLALVEENIPFEVIPGVTSP
ISVLNYAGIPITHRGLAQSFHIVTGMSARTLNVNWKALSKENGTLVFMMGLSNLETIVEK
LLENGKDIETPCGVVMRGTTSKQRKVIGTLENICKKVREAKLESPCIIVVGDVVSLNEKL
SWYENLPLFGANICLTRSKEQSKEIKWKLKELGAEVTEINSIKIKETAYNLDEYINTLEK
YDHIVFTSVNAVNVFFDYLVKNRVDIRKIKADFAVLGKATKKALIARGIVPSIMAHSFTA
EGLFEVLKDNIKEGEEVLIPCSSLSREYLFDNLASLGAKCHRVNIYDTICGDVKNPRAFK
EVDMVLYTSPSTVKNMIDMIGLEALKEKVSIAIGPITLKALNESGIEGKMCKTHCGDGFL
SEIEGIWQEVKK
Enzyme 3 Number of Residues 492
Enzyme 3 Molecular Weight 54468
Enzyme 3 Theoretical pI 6.70
Enzyme 3 GO Classification
Function
  • C-methyltransferase activity
  • carbon-oxygen lyase activity
  • catalytic activity
  • hydro-lyase activity
  • lyase activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • uroporphyrin-III C-methyltransferase activity
  • uroporphyrinogen-III synthase activity
Process
  • cellular metabolism
  • cobalamin biosynthesis
  • heme biosynthesis
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin biosynthesis
  • porphyrin metabolism
Component
—
Enzyme 3 General Function Coenzyme transport and metabolism
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions
  • hydroxymethylbilane = uroporphyrinogen III + H2O [RN:R03165] ALL_REAC R03165
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID Q0TQG5 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name Q0TQG5_CLOP1 Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID CP000246 Link Image
Enzyme 3 GeneCard ID Not Available
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 15859
Enzyme 4 Name Uroporphyrinogen-III methyltransferase/synthase (EC 4.2.1.75) (EC 2.1.1.107)
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name hemD
Enzyme 4 Protein Sequence >Uroporphyrinogen-III methyltransferase/synthase (EC 4.2.1.75) (EC 2.1.1.107) 
MSKKAYIIGAGPGDEELLTLKAINALQKCTAVLYDRLVGNNILNYLNDDCEIYYCGKEPG
CHYKTQEEINESIVELAKKGHIVGRVKGGDPYVFGRGGEEVLALVEENIPFEVIPGVTSP
ISVLNYAGIPITHRGLAQSFHIVTGMSARTLNVNWKALSKENGTLVFMMGLSNLETIVEK
LLENGKDIETPCGVVMRGTTSKQRKVIGTLENICKKVREAKLESPCIIVVGDVVSLNEKL
SWYEKLPLFGANICLTRSKEQSKEIKWKLKELGAEVTEINSIKIKETSENLDEYINTLEK
YDHIVFTSVNAVNVFFDYLVKKRVDIRKIKADFAVLGKATKKALIARGIVPSIMAHSFTA
EGLFEVLKDNIKEGEEVLIPCSSLSREYLFDNLASLGAKCHRVNIYDTICGDVKNPRAFK
EVDMVLYTSPSTVKNMIDMIGLESLKEKVSIAIGPITLKALNESGIEGKMCKTHCGDGFL
SEIEGIWQEVKK
Enzyme 4 Number of Residues 492
Enzyme 4 Molecular Weight 54508
Enzyme 4 Theoretical pI 6.90
Enzyme 4 GO Classification
Function
  • C-methyltransferase activity
  • carbon-oxygen lyase activity
  • catalytic activity
  • hydro-lyase activity
  • lyase activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • uroporphyrin-III C-methyltransferase activity
  • uroporphyrinogen-III synthase activity
Process
  • cellular metabolism
  • cobalamin biosynthesis
  • heme biosynthesis
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin biosynthesis
  • porphyrin metabolism
Component
—
Enzyme 4 General Function Coenzyme transport and metabolism
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions
  • hydroxymethylbilane = uroporphyrinogen III + H2O [RN:R03165] ALL_REAC R03165
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID Q0ST17 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name Q0ST17_CLOPS Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID CP000312 Link Image
Enzyme 4 GeneCard ID Not Available
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 15860
Enzyme 5 Name Siroheme synthase
Enzyme 5 Synonyms
  1. Uroporphyrinogen-III C-methyltransferase
  2. Urogen III methylase
  3. SUMT
  4. Uroporphyrinogen III methylase
  5. UROM
  6. Precorrin-2 dehydrogenase
  7. Sirohydrochlorin ferrochelatase
Enzyme 5 Gene Name cysG
Enzyme 5 Protein Sequence >Siroheme synthase 
MDHLPIFCQLRDRDCLIVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTL
VEGPFDESLLDTCWLAIAATDDDALNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRS
PLMVAVSSGGTSPVLARLLREKLESLLPLHLGQVAKYAGQLRGRVKQQFATMGERRRFWE
KLFVNDRLAQSLANNDQKAITETTEQLINEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQ
QADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLK
GGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLITGHL
KTGGELDWENLAAEKQTLVFYMGLNQAATIQQKLIEHGMPGEMPVAIVENGTAVTQRVID
GTLTQLGELAQQMNSPSLIIIGRVVGLRDKLNWFSNH
Enzyme 5 Number of Residues 457
Enzyme 5 Molecular Weight 49952
Enzyme 5 Theoretical pI 6.13
Enzyme 5 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • cellular metabolism
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin biosynthesis
  • porphyrin metabolism
Component
—
Enzyme 5 General Function Coenzyme transport and metabolism
Enzyme 5 Specific Function Multifunctional enzyme that catalyze the SAM-dependent methylation of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 and then position C-12 or C-18 to form trimethylpyrrocorphin 2. It also catalyzes the conversion of precorrin-2 into siroheme. This reaction consist of the NAD- dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID P0AEA8 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name CYSG_ECOLI Link Image
Enzyme 5 PDB ID 1PJT Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID X14202 Link Image
Enzyme 5 GeneCard ID Not Available
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Bell AI, Gaston KL, Cole JA, Busby SJ: Cloning of binding sequences for the Escherichia coli transcription activators, FNR and CRP: location of bases involved in discrimination between FNR and CRP. Nucleic Acids Res. 1989 May 25;17(10):3865-74. [PubMed Link Image]
  2. Peakman T, Crouzet J, Mayaux JF, Busby S, Mohan S, Harborne N, Wootton J, Nicolson R, Cole J: Nucleotide sequence, organisation and structural analysis of the products of genes in the nirB-cysG region of the Escherichia coli K-12 chromosome. Eur J Biochem. 1990 Jul 31;191(2):315-23. [PubMed Link Image]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed Link Image]
  4. Warren MJ, Stolowich NJ, Santander PJ, Roessner CA, Sowa BA, Scott AI: Enzymatic synthesis of dihydrosirohydrochlorin (precorrin-2) and of a novel pyrrocorphin by uroporphyrinogen III methylase. FEBS Lett. 1990 Feb 12;261(1):76-80. [PubMed Link Image]
  5. Warren MJ, Roessner CA, Santander PJ, Scott AI: The Escherichia coli cysG gene encodes S-adenosylmethionine-dependent uroporphyrinogen III methylase. Biochem J. 1990 Feb 1;265(3):725-9. [PubMed Link Image]
  6. Spencer JB, Stolowich NJ, Roessner CA, Scott AI: The Escherichia coli cysG gene encodes the multifunctional protein, siroheme synthase. FEBS Lett. 1993 Nov 29;335(1):57-60. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 15861
Enzyme 6 Name Putative uroporphyrinogen-III C-methyltransferase
Enzyme 6 Synonyms
  1. Urogen III methylase
  2. ORF X
Enzyme 6 Gene Name hemX
Enzyme 6 Protein Sequence >Putative uroporphyrinogen-III C-methyltransferase 
MTEQEKTSAVVEETREAVDTTSQPVATEKKSKNNTALILSAVAIAIALAAGIGLYGWGKQ
QAVNQTATSDALANQLTALQKAQESQKAELEGIIKQQAAQLKQANRQQETLAKQLDEVQQ
KVATISGSDAKTWLLAQADFLVKLAGRKLWSDQDVTTAAALLKSADASLADMNDPSLITV
RRAITDDIASLSAVSQVDYDGIILKLNQLSNQVDNLRLADNDSDGSPMDSDGEELSSSIS
EWRINLQKSWQNFMDNFITIRRRDDTAVPLLAPNQDIYLRENIRSRLLVAAQAVPRHQEE
TYRQALENVSTWVRAYYDTDDATTKAFLDEVDQLSQQNISMDLPETLQSQAMLEKLMQTR
VRNLLAQPAAGTTEAKPAPAPQADTPAAAPQGE
Enzyme 6 Number of Residues 393
Enzyme 6 Molecular Weight 42963
Enzyme 6 Theoretical pI 4.41
Enzyme 6 GO Classification Not Available
Enzyme 6 General Function Coenzyme transport and metabolism
Enzyme 6 Specific Function S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 37-57
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein Not Available
Enzyme 6 UniProtKB/Swiss-Prot ID P09127 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name HEMX_ECOLI Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence Not Available
Enzyme 6 GenBank Gene ID X13406 Link Image
Enzyme 6 GeneCard ID Not Available
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Sasarman A, Echelard Y, Letowski J, Tardif D, Drolet M: Nucleotide sequence of the hemX gene, the third member of the Uro operon of Escherichia coli K12. Nucleic Acids Res. 1988 Dec 23;16(24):11835. [PubMed Link Image]
  2. Alefounder PR, Abell C, Battersby AR: The sequence of hemC, hemD and two additional E. coli genes. Nucleic Acids Res. 1988 Oct 25;16(20):9871. [PubMed Link Image]
  3. Daniels DL, Plunkett G 3rd, Burland V, Blattner FR: Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes. Science. 1992 Aug 7;257(5071):771-8. [PubMed Link Image]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed Link Image]
  5. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 16700
Enzyme 7 Name Fused siroheme synthase 1,3-dimethyluroporphyriongen III dehydrogenase and siroheme ferrochelatase
Enzyme 7 Synonyms
  1. uroporphyrinogen methyltransferase
Enzyme 7 Gene Name cysG
Enzyme 7 Protein Sequence >Fused siroheme synthase 1,3-dimethyluroporphyriongen III dehydrogenase and siroheme ferrochelatase 
MDHLPIFCQLRDRDCLIVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTL
VEGPFDESLLDTCWLAIAATDDDALNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRS
PLMVAVSSGGTSPVLARLLREKLESLLPLHLGQVAKYAGQLRGRVKQQFATMGERRRFWE
KLFVNDRLAQSLANNDQKAITETTEQLINEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQ
QADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLK
GGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLITGHL
KTGGELDWENLAAEKQTLVFYMGLNQAATIQQKLIEHGMPGEMPVAIVENGTAVTQRVID
GTLTQLGELAQQMNSPSLIIIGRVVGLRDKLNWFSNH
Enzyme 7 Number of Residues 457
Enzyme 7 Molecular Weight 49952
Enzyme 7 Theoretical pI 6.13
Enzyme 7 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • cellular metabolism
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin biosynthesis
  • porphyrin metabolism
Component
—
Enzyme 7 General Function Coenzyme transport and metabolism
Enzyme 7 Specific Function Multifunctional enzyme that catalyze the SAM-dependent methylation of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 and then position C-12 or C-18 to form trimethylpyrrocorphin 2. It also catalyzes the conversion of precorrin-2 into siroheme. This reaction consist of the NAD- dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein Not Available
Enzyme 7 UniProtKB/Swiss-Prot ID B1X716 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name B1X716_ECODH Link Image
Enzyme 7 PDB ID 1PJT Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence Not Available
Enzyme 7 GenBank Gene ID CP000948 Link Image
Enzyme 7 GeneCard ID Not Available
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
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