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Human Metabolome Database Version 2.5

 

Showing metabocard for 17a-Hydroxypregnenolone (HMDB00363)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-06-10 16:30:02
Accession Number HMDB00363
Secondary Accession Numbers Not Available
Common Name 17a-Hydroxypregnenolone
Description 17a-Hydroxypregnenolone is a 21-carbon steroid that is converted from pregnenolone by cytochrome P450 17alpha hydroxylase/C17,20 lyase (CYP17, EC 1.14.99.9). 17a-Hydroxypregnenolone is an intermediate in the delta-5 pathway of biosynthesis of gonadal steroid hormones and the adrenal corticosteroids. The first, rate-limiting and hormonally regulated step in the biosynthesis of all steroid hormones is the conversion of cholesterol to pregnenolone. The conversion of cholesterol to pregnenolone is accomplished by the cleavage of the cholesterol side chain, catalyzed by a mitochondrial cytochrome P450 enzyme termed P450scc where scc designates Side Chain Cleavage. All steroid hormones are made from the pregnenolone produced by P450scc; thus, the presence or absence of each of the activities of CYP17 directs this pregnenolone towards its final metabolic pathway. While all cytochrome P450 enzymes can catalyze multiple reactions on a single active site, CYP17 is the only one described to date in which these multiple activities are differentially regulated by a physiologic process. 17a-Hydroxypregnenolone is converted to dehydroepiandrosterone by the 17,20 lyase activity of CYP17. The ratio of the 17,20 lyase to 17 alpha-hydroxylase activity of CYP17 determines the ratio of C21 to C19 steroids produced. This ratio is regulated post-translationally by at least three factors: the abundance of the electron-donating protein P450 oxidoreductase, the presence of cytochrome b5, and the serine phosphorylation of CYP17. (PMID: 12573809)
Synonyms
  1. 17-Hydroxy-D5-pregnenolone
  2. 17-Hydroxypregnenolone
  3. 17a-Hydroxypregnolone
  4. 17alpha-hydroxypregnenolone
  5. 17-OH-pregnenolone
  6. 3b,17-Dihydroxy-5-pregnen-20-one
  7. 3b,17-dihydroxy-Pregn-5-en-20-one
  8. 3b,17a-Dihydroxypregn-5-en-20-one
  9. 5-Pregnen-3b,17a-diol-20-one;17alpha-Hydroxypregnanolone
Chemical IUPAC Name 1-[(3S,8R,9S,10R,13S,17R)-3,17-dihydroxy-10,13-dimethyl-1,2,3,4,7,8,9,11,12,14,15,16-dodecahydrocyclopenta[a]phenanthren-17-yl]ethanone
Chemical Formula C21H32O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Cholesterols and derivatives
Class
  • Steroids and Steroid Derivatives
Sub Class
  • Ketosteroids
Family
  • Mammalian Metabolite
Species
  • ketone
  • secondary alcohol
  • tertiary alcohol
  • alkene
Biofunction
  • Hormones, Membrane component
Application
—
Source
  • Endogenous
Average Molecular Weight 332.477
Monoisotopic Molecular Weight 332.235138
Isomeric SMILES CC(=O)[C@@]1(O)CC[C@H]2[C@@H]3CC=C4C[C@@H](O)CC[C@]4(C)[C@H]3CC[C@]12C
Canonical SMILES CC(=O)C1(O)CCC2C3CC=C4CC(O)CCC4(C)C3CCC12C
KEGG Compound ID C05138 Link Image
BioCyc ID Not Available
BiGG ID 45199 Link Image
Wikipedia Link 17-Hydroxypregnenolone Link Image
NuGOwiki Link HMDB00363 Link Image
Metagene Link HMDB00363 Link Image
METLIN ID 5352 Link Image
PubChem Compound 440573 Link Image
PubChem Substance 7557 Link Image
ChEBI ID 28750 Link Image
CAS Registry Number 387-79-1
InChI Identifier InChI=1/C21H32O3/c1-13(22)21(24)11-8-18-16-5-4-14-12-15(23)6-9-19(14,2)17(16)7-10-20(18,21)3/h4,15-18,23-24H,5-12H2,1-3H3/t15-,16+,17-,18-,19-,20-,21-/m0/s1
Synthesis Reference Kaspar, Emanuel; Hiersemann, Wolfgang; Schenck, Martin. Preparation from their esters of steroid alcohols that are sensitive to acids and alkali. (1958), DE 1028572 19580424 CAN 54:74845 AN 1960:74845 CAPLUS
Melting Point (Experimental) 266-271 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.0377 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 3.15 [Predicted by ALOGPS]; 3 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
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
  • Membrane (Predicted from LogP)
  • Cytoplasm
  • endoplasmic reticulum
Biofluid Location
  • Blood
Tissue Location
Tissue References
Adrenal Cortex —
Testes —
Concentrations (Normal)
Biofluid Blood
Value 0.003 (0.000 - 0.006) uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Kushnir MM, Rockwood AL, Roberts WL, Pattison EG, Owen WE, Bunker AM, Meikle AW: Development and performance evaluation of a tandem mass spectrometry assay for 4 adrenal steroids. Clin Chem. 2006 Aug;52(8):1559-67. Epub 2006 Jun 15. [PubMed Link Image]
Biofluid Blood
Value 0.006 (0.001-0.012) uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Kushnir MM, Rockwood AL, Roberts WL, Pattison EG, Owen WE, Bunker AM, Meikle AW: Development and performance evaluation of a tandem mass spectrometry assay for 4 adrenal steroids. Clin Chem. 2006 Aug;52(8):1559-67. Epub 2006 Jun 15. [PubMed Link Image]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Androgen and Estrogen Metabolism SMP00068 Link Image map00150 Link Image
Steroidogenesis SMP00130 Link Image map00140 Link Image
General References
  1. Shimozawa K, Saisho S, Yata J, Kambegawa A: Age-related changes in serum 17-hydroxypregnenolone and 17-hydroxypregnenolone sulfate concentrations in human infancy and childhood. Endocrinol Jpn. 1988 Apr;35(2):189-95. [PubMed Link Image]
  2. Rodriguez-Rigau LJ, Weiss DB, Smith KD, Steinberger E: Suggestion of abnormal testicular steroidogenesis in some oligospermic men. Acta Endocrinol (Copenh). 1978 Feb;87(2):400-12. [PubMed Link Image]
  3. Kaufman FR, Costin G, Goebelsmann U, Stanczyk FZ, Zachmann M: Male pseudohermaphroditism due to 17,20-desmolase deficiency. J Clin Endocrinol Metab. 1983 Jul;57(1):32-6. [PubMed Link Image]
  4. Wikipedia Link Image
Metabolic Enzymes
  1. 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I
  2. Cytochrome P450 17A1
  3. cDNA FLJ75712, highly similar to Homo sapiens hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 1
  4. cDNA FLJ76435, highly similar to Homo sapiens cytochrome P450, family 11, subfamily A, polypeptide 1
  5. Cytochrome P450 21-hydroxylase
  6. HSD3B2 protein
  7. Cytochrome P450, family 21, subfamily A, polypeptide 2
Enzyme 1 [top]
Enzyme 1 ID 5738
Enzyme 1 Name 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I
Enzyme 1 Synonyms
  1. 3- beta-HSD I
  2. Trophoblast antigen FDO161G[Includes: 3-beta-hydroxy- Delta(5-steroid dehydrogenase
  3. 3-beta-hydroxy-5-ene steroid dehydrogenase
  4. Progesterone reductase
  5. Steroid Delta- isomerase
  6. Delta-5-3-ketosteroid isomerase]
Enzyme 1 Gene Name HSD3B1
Enzyme 1 Protein Sequence >4-isomerase type I 
MTGWSCLVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPELREEFSKLQNKTKLTVLE
GDILDEPFLKRACQDVSVIIHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVF
IYTSSIEVAGPNSYKEIIQNGHEEEPLENTWPAPYPHSKKLAEKAVLAANGWNLKNGGTL
YTCALRPMYIYGEGSRFLSASINEALNNNGILSSVGKFSTVNPVYVGNVAWAHILALRAL
QDPKKAPSIRGQFYYISDDTPHQSYDNLNYTLSKEFGLRLDSRWSFPLSLMYWIGFLLEI
VSFLLRPIYTYRPPFNRHIVTLSNSVFTFSYKKAQRDLAYKPLYSWEEAKQKTVEWVGSL
VDRHKETLKSKTQ
Enzyme 1 Number of Residues 373
Enzyme 1 Molecular Weight 42252
Enzyme 1 Theoretical pI 8.98
Enzyme 1 GO Classification
Function
  • 3-beta-hydroxy-delta5-steroid dehydrogenase activity
  • catalytic activity
  • intramolecular oxidoreductase activity
  • intramolecular oxidoreductase activity, transposing C=C bonds
  • isomerase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
  • steroid dehydrogenase activity
  • steroid delta-isomerase activity
Process
  • cellular lipid metabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • steroid biosynthesis
  • steroid metabolism
Component
—
Enzyme 1 General Function Cell wall/membrane/envelope biogenesis
Enzyme 1 Specific Function 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids
Enzyme 1 Pathways
Enzyme 1 Reactions
  • A 3-oxo-delta5-steroid = a 3-oxo-delta4-steroid
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-13
Enzyme 1 Transmembrane Regions
  • 288-308
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 306889 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P14060 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name 3BHS1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1122 bp 
ATGACGGGCTGGAGCTGCCTTGTGACAGGAGCAGGAGGGTTTCTGGGACAGAGGATCATC
CGCCTCTTGGTGAAGGAGAAGGAGCTGAAGGAGATCAGGGTCTTGGACAAGGCCTTCGGA
CCAGAATTGAGAGAGGAATTTTCTAAACTCCAGAACAAGACCAAGCTGACAGTGCTGGAA
GGAGACATTCTGGATGAGCCATTCCTGAAGAGAGCCTGCCAGGACGTCTCGGTCATCATC
CACACCGCCTGTATCATTGATGTCTTCGGTGTCACTCACAGAGAGTCTATCATGAATGTC
AATGTGAAAGGTACCCAGCTCCTGTTAGAGGCCTGTGTCCAAGCTAGTGTGCCAGTCTTC
ATCTACACCAGTAGCATAGAGGTAGCCGGGCCCAACTCCTACAAGGAAATCATCCAGAAT
GGCCATGAAGAAGAGCCTCTGGAAAACACATGGCCCGCTCCATACCCACACAGCAAAAAG
CTTGCTGAGAAGGCTGTACTGGCGGCTAACGGGTGGAATCTGAAAAACGGCGGCACCCTG
TACACTTGTGCCTTACGACCCATGTATATCTATGGGGAAGGAAGCCGATTCCTTTCTGCT
AGTATAAACGAGGCCCTGAACAACAATGGGATCCTGTCAAGTGTTGGAAAGTTCTCCACT
GTTAACCCAGTCTATGTTGGCAATGTGGCCTGGGCCCACATTCTGGCCTTGAGGGCCCTG
CAGGACCCCAAGAAGGCCCCAAGCATCCGAGGACAGTTCTACTATATCTCAGATGACACG
CCTCACCAAAGCTATGATAACCTTAATTACACCCTGAGCAAAGAGTTCGGCCTCCGCCTT
GATTCCAGATGGAGCTTTCCTTTATCCCTGATGTATTGGATTGGCTTCCTGCTGGAAATA
GTGAGCTTCCTACTCAGGCCAATTTACACCTATCGACCGCCCTTCAACCGCCACATAGTC
ACATTGTCAAATAGCGTATTCACCTTCTCTTATAAGAAGGCTCAGCGAGATCTGGCGTAT
AAGCCACTCTACAGCTGGGAGGAAGCCAAGCAGAAAACGGTGGAGTGGGTTGGTTCCCTT
GTGGACCGGCACAAGGAGACCCTGAAGTCCAAGACTCAGTGA
Enzyme 1 GenBank Gene ID M27137 Link Image
Enzyme 1 GeneCard ID HSD3B1 Link Image
Enzyme 1 GenAtlas ID HSD3B1 Link Image
Enzyme 1 HGNC ID HGNC:5217 Link Image
Enzyme 1 Chromosome Location Not Available
Enzyme 1 Locus Not Available
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Luu The V, Lachance Y, Labrie C, Leblanc G, Thomas JL, Strickler RC, Labrie F: Full length cDNA structure and deduced amino acid sequence of human 3 beta-hydroxy-5-ene steroid dehydrogenase. Mol Endocrinol. 1989 Aug;3(8):1310-2. [PubMed Link Image]
  2. Lorence MC, Murry BA, Trant JM, Mason JI: Human 3 beta-hydroxysteroid dehydrogenase/delta 5----4isomerase from placenta: expression in nonsteroidogenic cells of a protein that catalyzes the dehydrogenation/isomerization of C21 and C19 steroids. Endocrinology. 1990 May;126(5):2493-8. [PubMed Link Image]
  3. Lorence MC, Corbin CJ, Kamimura N, Mahendroo MS, Mason JI: Structural analysis of the gene encoding human 3 beta-hydroxysteroid dehydrogenase/delta 5----4-isomerase. Mol Endocrinol. 1990 Dec;4(12):1850-5. [PubMed Link Image]
  4. Lachance Y, Luu-The V, Labrie C, Simard J, Dumont M, de Launoit Y, Guerin S, Leblanc G, Labrie F: Characterization of human 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4-isomerase gene and its expression in mammalian cells. J Biol Chem. 1990 Nov 25;265(33):20469-75. [PubMed Link Image]
  5. Nickson DA, McBride MW, Zeinali S, Hawes CS, Petropoulos A, Mueller UW, Sutcliffe RG: Molecular cloning and expression of human trophoblast antigen FDO161G and its identification as 3 beta-hydroxy-5-ene steroid dehydrogenase. J Reprod Fertil. 1991 Sep;93(1):149-56. [PubMed Link Image]
  6. Dumont M, Luu-The V, Dupont E, Pelletier G, Labrie F: Characterization, expression, and immunohistochemical localization of 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase in human skin. J Invest Dermatol. 1992 Oct;99(4):415-21. [PubMed Link Image]
  7. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6332
Enzyme 2 Name Cytochrome P450 17A1
Enzyme 2 Synonyms
  1. CYPXVII
  2. P450-C17
  3. P450c17
  4. Steroid 17-alpha-monooxygenase
  5. Steroid 17-alpha-hydroxylase/17,20 lyase
Enzyme 2 Gene Name CYP17A1
Enzyme 2 Protein Sequence >Cytochrome P450 17A1 
MWELVALLLLTLAYLFWPKRRCPGAKYPKSLLSLPLVGSLPFLPRHGHMHNNFFKLQKKY
GPIYSVRMGTKTTVIVGHHQLAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFADSGAH
WQLHRRLAMATFALFKDGDQKLEKIICQEISTLCDMLATHNGQSIDISFPVFVAVTNVIS
LICFNTSYKNGDPELNVIQNYNEGIIDNLSKDSLVDLVPWLKIFPNKTLEKLKSHVKIRN
DLLNKILENYKEKFRSDSITNMLDTLMQAKMNSDNGNAGPDQDSELLSDNHILTTIGDIF
GAGVETTTSVVKWTLAFLLHNPQVKKKLYEEIDQNVGFSRTPTISDRNRLLLLEATIREV
LRLRPVAPMLIPHKANVDSSIGEFAVDKGTEVIINLWALHHNEKEWHQPDQFMPERFLNP
AGTQLISPSVSYLPFGAGPRSCIGEILARQELFLIMAWLLQRFDLEVPDDGQLPSLEGIP
KVVFLIDSFKVKIKVRQAWREAQAEGST
Enzyme 2 Number of Residues 508
Enzyme 2 Molecular Weight 57371
Enzyme 2 Theoretical pI 8.87
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • tetrapyrrole binding
  • transition metal ion binding
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 2 Specific Function Conversion of pregnenolone and progesterone to their 17- alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. Catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction. Involved in sexual development during fetal life and at puberty
Enzyme 2 Pathways
Enzyme 2 Reactions
  • a steroid + AH2 + O2 = a 17alpha-hydroxysteroid + A + H2O
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-24
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 181342 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P05093 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name CP17A_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1527 bp 
ATGTGGGAGCTCGTGGCTCTCTTGCTGCTTACCCTAGCTTATTTGTTTTGGCCCAAGAGA
AGGTGCCCTGGTGCCAAGTACCCCAAGAGCCTCCTGTCCCTGCCCCTGGTGGGCAGCCTG
CCATTCCTCCCCAGACATGGCCATATGCATAACAACTTCTTCAAGCTGCAGAAAAAATAT
GGCCCCATCTATTCTGTTCGTATGGGCACCAAGACTACAGTGATTGTCGGCCACCACCAG
CTGGCCAAGGAGGTGCTTATTAAGAAGGGCAAGGACTTCTCTGGGCGGCCTCAAATGGCA
ACTCTAGACATCGCGTCCAACAACCGTAAGGGTATCGCCTTCGCTGACTCTGGCGCACAC
TGGCAGCTGCATCGAAGGCTGGCGATGGCCACCTTTGCCCTGTTCAAGGATGGCGATCAG
AAGCTGGAGAAGATCATTTGTCAGGAAATCAGTACATTGTGTGATATGCTGGCCACCCAC
AACGGACAGTCCATAGACATCTCCTTTCCTGTCTTCGTGGCGGTAACCAATGTCATCTCC
TTGATCTGCTTCAATACCTCCTACAAGAATGGGGACCCTGAGTTGAATGTCATACAGAAT
TACAATGAAGGCATCATAGACAACCTGAGCAAAGACAGCCTGGTGGACCTAGTCCCCTGG
TTGAAGATTTTCCCCAACAAAACCCTGGAAAAATTAAAGAGCCATGTTAAAATACGAAAT
GATCTGCTGAATAAAATACTTGAAAATTACAAGGAGAAATTCCGGAGTGACTCTATCACC
AACATGCTGGACACACTGATGCAAGCCAAGATGAACTCAGATAATGGCAATGCTGGCCCA
GATCAAGATTCAGAGCTGCTTTCAGATAACCACATTCTCACCACCATAGGGGACATCTTT
GGGGCTGGCGTGGAGACCACCACCTCTGTGGTTAAATGGACCCTGGCCTTCCTGCTGCAC
AATCCTCAGGTGAAGAAGAAGCTCTACGAGGAGATTGACCAGAATGTGGGTTTCAGCCGC
ACACCAACTATCAGTGACCGTAACCGTCTCCTCCTGCTGGAGGCCACCATCCGAGAGGTG
CTTCGCCTCAGGCCCGTGGCCCCTATGCTCATCCCCCACAAGGCCAACGTTGACTCCAGC
ATCGGTGAGTTTGCTGTGGACAAGGGCACAGAAGTTATCATCAATCTGTGGGCGCTGCAT
CACAATGAGAAGGAGTGGCACCAGCCGGATCAGTTCATGCCTGAGCGTTTCTTGAATCCA
GCGGGGACCCAGCTCATCTCACCGTCAGTAAGCTATTTGCCCTTCGGAGCAGGACCTCGC
TCCTGTATAGGTGAGATCCTGGCCCGCCAGGAGCTCTTCCTCATCATGGCCTGGCTGCTG
CAGAGGTTCGACCTGGAGGTGCCAGATGATGGGCAGCTGCCCTCCCTGGAAGGCATCCCC
AAGGTGGTCTTTCTGATCGACTCTTTCAAAGTGAAGATCAAGGTGCGCCAGGCCTGGAGG
GAAGCCCAGGCTGAGGGTAGCACCTAA
Enzyme 2 GenBank Gene ID M14564 Link Image
Enzyme 2 GeneCard ID CYP17A1 Link Image
Enzyme 2 GenAtlas ID CYP17A1 Link Image
Enzyme 2 HGNC ID HGNC:2593 Link Image
Enzyme 2 Chromosome Location 10
Enzyme 2 Locus 10q24.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Chung BC, Picado-Leonard J, Haniu M, Bienkowski M, Hall PF, Shively JE, Miller WL: Cytochrome P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): cloning of human adrenal and testis cDNAs indicates the same gene is expressed in both tissues. Proc Natl Acad Sci U S A. 1987 Jan;84(2):407-11. [PubMed Link Image]
  2. Picado-Leonard J, Miller WL: Cloning and sequence of the human gene for P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): similarity with the gene for P450c21. DNA. 1987 Oct;6(5):439-48. [PubMed Link Image]
  3. Bradshaw KD, Waterman MR, Couch RT, Simpson ER, Zuber MX: Characterization of complementary deoxyribonucleic acid for human adrenocortical 17 alpha-hydroxylase: a probe for analysis of 17 alpha-hydroxylase deficiency. Mol Endocrinol. 1987 May;1(5):348-54. [PubMed Link Image]
  4. Brentano ST, Picado-Leonard J, Mellon SH, Moore CC, Miller WL: Tissue-specific, cyclic adenosine 3',5'-monophosphate-induced, and phorbol ester-repressed transcription from the human P450c17 promoter in mouse cells. Mol Endocrinol. 1990 Dec;4(12):1972-9. [PubMed Link Image]
  5. Kagimoto M, Winter JS, Kagimoto K, Simpson ER, Waterman MR: Structural characterization of normal and mutant human steroid 17 alpha-hydroxylase genes: molecular basis of one example of combined 17 alpha-hydroxylase/17,20 lyase deficiency. Mol Endocrinol. 1988 Jun;2(6):564-70. [PubMed Link Image]
  6. Auchus RJ, Miller WL: Molecular modeling of human P450c17 (17alpha-hydroxylase/17,20-lyase): insights into reaction mechanisms and effects of mutations. Mol Endocrinol. 1999 Jul;13(7):1169-82. [PubMed Link Image]
  7. Yanase T, Kagimoto M, Suzuki S, Hashiba K, Simpson ER, Waterman MR: Deletion of a phenylalanine in the N-terminal region of human cytochrome P-450(17 alpha) results in partial combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Biol Chem. 1989 Oct 25;264(30):18076-82. [PubMed Link Image]
  8. Lin D, Harikrishna JA, Moore CC, Jones KL, Miller WL: Missense mutation serine106----proline causes 17 alpha-hydroxylase deficiency. J Biol Chem. 1991 Aug 25;266(24):15992-8. [PubMed Link Image]
  9. Yanase T, Waterman MR, Zachmann M, Winter JS, Simpson ER, Kagimoto M: Molecular basis of apparent isolated 17,20-lyase deficiency: compound heterozygous mutations in the C-terminal region (Arg(496)----Cys, Gln(461)----Stop) actually cause combined 17 alpha-hydroxylase/17,20-lyase deficiency. Biochim Biophys Acta. 1992 Aug 25;1139(4):275-9. [PubMed Link Image]
  10. Ahlgren R, Yanase T, Simpson ER, Winter JS, Waterman MR: Compound heterozygous mutations (Arg 239----stop, Pro 342----Thr) in the CYP17 (P45017 alpha) gene lead to ambiguous external genitalia in a male patient with partial combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Clin Endocrinol Metab. 1992 Mar;74(3):667-72. [PubMed Link Image]
  11. Imai T, Globerman H, Gertner JM, Kagawa N, Waterman MR: Expression and purification of functional human 17 alpha-hydroxylase/17,20-lyase (P450c17) in Escherichia coli. Use of this system for study of a novel form of combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Biol Chem. 1993 Sep 15;268(26):19681-9. [PubMed Link Image]
  12. Monno S, Ogawa H, Date T, Fujioka M, Miller WL, Kobayashi M: Mutation of histidine 373 to leucine in cytochrome P450c17 causes 17 alpha-hydroxylase deficiency. J Biol Chem. 1993 Dec 5;268(34):25811-7. [PubMed Link Image]
  13. Fardella CE, Zhang LH, Mahachoklertwattana P, Lin D, Miller WL: Deletion of amino acids Asp487-Ser488-Phe489 in human cytochrome P450c17 causes severe 17 alpha-hydroxylase deficiency. J Clin Endocrinol Metab. 1993 Aug;77(2):489-93. [PubMed Link Image]
  14. Fardella CE, Hum DW, Homoki J, Miller WL: Point mutation of Arg440 to His in cytochrome P450c17 causes severe 17 alpha-hydroxylase deficiency. J Clin Endocrinol Metab. 1994 Jul;79(1):160-4. [PubMed Link Image]
  15. Laflamme N, Leblanc JF, Mailloux J, Faure N, Labrie F, Simard J: Mutation R96W in cytochrome P450c17 gene causes combined 17 alpha-hydroxylase/17-20-lyase deficiency in two French Canadian patients. J Clin Endocrinol Metab. 1996 Jan;81(1):264-8. [PubMed Link Image]
  16. Biason-Lauber A, Kempken B, Werder E, Forest MG, Einaudi S, Ranke MB, Matsuo N, Brunelli V, Schonle EJ, Zachmann M: 17alpha-hydroxylase/17,20-lyase deficiency as a model to study enzymatic activity regulation: role of phosphorylation. J Clin Endocrinol Metab. 2000 Mar;85(3):1226-31. [PubMed Link Image]
  17. Gupta MK, Geller DH, Auchus RJ: Pitfalls in characterizing P450c17 mutations associated with isolated 17,20-lyase deficiency. J Clin Endocrinol Metab. 2001 Sep;86(9):4416-23. [PubMed Link Image]
  18. Di Cerbo A, Biason-Lauber A, Savino M, Piemontese MR, Di Giorgio A, Perona M, Savoia A: Combined 17alpha-Hydroxylase/17,20-lyase deficiency caused by Phe93Cys mutation in the CYP17 gene. J Clin Endocrinol Metab. 2002 Feb;87(2):898-905. [PubMed Link Image]
  19. Van Den Akker EL, Koper JW, Boehmer AL, Themmen AP, Verhoef-Post M, Timmerman MA, Otten BJ, Drop SL, De Jong FH: Differential inhibition of 17alpha-hydroxylase and 17,20-lyase activities by three novel missense CYP17 mutations identified in patients with P450c17 deficiency. J Clin Endocrinol Metab. 2002 Dec;87(12):5714-21. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 12986
Enzyme 3 Name cDNA FLJ75712, highly similar to Homo sapiens hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 1
Enzyme 3 Synonyms
  1. HSD3B1, mRNA
Enzyme 3 Gene Name Not Available
Enzyme 3 Protein Sequence >cDNA FLJ75712, highly similar to Homo sapiens hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 1 
MTGWSCLVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPELREEFSKLQNKTKLTVLE
GDILDEPFLKRACQDVSVIIHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVF
IYTSSIEVAGPNSYKEIIQNGHEEEPLENTWPAPYPHSKKLAEKAVLAANGWNLKNGGTL
YTCALRPMYIYGEGSRFLSASINEALNNNGILSSVGKFSTVNPVYVGNVAWAHILALRAL
QDPKKAPSIRGQFYYISDDTPHQSYDNLNYTLSKEFGLRLDSRWSFPLSLMYWIGFLLEI
VSFLLRPIYTYRPPFNRHIVTLSNSVFTFSYKKAQRDLAYKPLYSWEEAKQKTVEWVGSL
VDRHKETLKSKTQ
Enzyme 3 Number of Residues 373
Enzyme 3 Molecular Weight 42252
Enzyme 3 Theoretical pI 8.98
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Cell wall/membrane/envelope biogenesis
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function Not Available
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 158256544 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID A8K691 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name A8K691_HUMAN 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 AK291556 Link Image
Enzyme 3 GeneCard ID A8K691 Link Image
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 Not Available
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 13012
Enzyme 4 Name cDNA FLJ76435, highly similar to Homo sapiens cytochrome P450, family 11, subfamily A, polypeptide 1
Enzyme 4 Synonyms
  1. CYP11A1, mRNA
  2. Cytochrome P450, family 11, subfamily A, polypeptide 1, isoform CRA_b
Enzyme 4 Gene Name CYP11A1
Enzyme 4 Protein Sequence >cDNA FLJ76435, highly similar to Homo sapiens cytochrome P450, family 11, subfamily A, polypeptide 1 
MLAKGLPPRSVLVKGCQTFLSAPREGLGRLRVPTGEGAGISTRSPRPFNEIPSPGDNGWL
NLYHFWRETGTHKVHLHHVQNFQKYGPIYREKLGNVESVYVIDPEDVALLFKSEGPNPER
FLIPPWVAYHQYYQRPIGVLLKKSAAWKKDRVALNQEVMAPEATKNFLPLLDAVSRDFVS
VLHRRIKKAGSGNYSGDISDDLFRFAFESITNVIFGERQGMLEEVVNPEAQRFIDAIYQM
FHTSVPMLNLPPDLFRLFRTKTWKDHVAAWDVIFSKADIYTQNFYWELRQKGSVHHDYRG
ILYRLLGDSKMSFEDIKANVTEMLAGGVDTTSMTLQWHLYEMARNLKVQDMLRAEVLAAR
HQAQGDMATMLQLVPLLKASIKETLRLHPISVTLQRYLVNDLVLRDYMIPAKTLVQVAIY
ALGREPTFFFDPENFDPTRWLSKDKNITYFRNLGFGWGVRQCLGRRIAELEMTIFLINML
ENFRVEIQHLSDVGTTFNLILMPEKPISFTFWPFNQEATQQ
Enzyme 4 Number of Residues 521
Enzyme 4 Molecular Weight 60103
Enzyme 4 Theoretical pI 9.18
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Secondary metabolites biosynthesis, transport and catabolism
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 158258032 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID A8K8D5 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name A8K8D5_HUMAN 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 AK292300 Link Image
Enzyme 4 GeneCard ID A8K8D5 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 13013
Enzyme 5 Name Cytochrome P450 21-hydroxylase
Enzyme 5 Synonyms
  1. Cytochrome P450, family 21, subfamily A, polypeptide 2, isoform CRA_b
  2. Cytochrome P450, family 21, subfamily A, polypeptide 2
  3. DJ34F7.3
  4. Cytochrome P450, subfamily XXIA
  5. Steroid 21-hydroxylase, congenital adrenal hyperplasia, polypeptide 2
  6. CYP21, P450c21B
Enzyme 5 Gene Name P450-CYP21B
Enzyme 5 Protein Sequence >Cytochrome P450 21-hydroxylase 
MLLLGLLLLLPLLAGARLLWNWWKLRSLHLPPLAPGFLHLLQPDLPIYLLGLTQKFGPIY
RLHLGLQDVVVLNSKRTIEEAMVKKWADFAGRPEPLTYKLVSRNYPDLSLGDYSLLWKAH
KKLTRSALLLGIRDSMEPVVEQLTQEFCERMRAQPGTPVAIEEEFSLLTCSIICYLTFGD
KIKDDNLMPAYYKCIQEVLKTWSHWSIQIVDVIPFLRFFPNPGLRRLKQAIEKRDHIVEM
QLRQHKESLVAGQWRDMMDYMLQGVAQPSMEEGSGQLLEGHVHMAAVDLLIGGTETTANT
LSWAVVFLLHHPEIQQRLQEELDHELGPGASSSRVPYKDRARLPLLNATIAEVLRLRPVV
PLALPHRTTRPSSISGYDIPEGTVIIPNLQGAHLDETVWERPHEFWPDRFLEPGKNSRAL
AFGCGARVCLGEPLARLELFVVLTRLLQAFTLLPSGDALPSLQPLPHCSVILKMQPFQVR
LQPRGMGAHSPGQSQ
Enzyme 5 Number of Residues 495
Enzyme 5 Molecular Weight 56002
Enzyme 5 Theoretical pI 7.90
Enzyme 5 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • tetrapyrrole binding
  • transition metal ion binding
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 5 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 5 Specific Function Not Available
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 Q16874 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name Q16874_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AF019413 Link Image
Enzyme 5 GeneCard ID Q16874 Link Image
Enzyme 5 GenAtlas ID P450-CYP21B Link Image
Enzyme 5 HGNC ID HGNC:2600 Link Image
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 14860
Enzyme 6 Name HSD3B2 protein
Enzyme 6 Synonyms
  1. Hydroxy-delta-5-steroid dehydrogenase, 3 beta-and steroid delta-isomerase 2, isoform CRA_a
Enzyme 6 Gene Name HSD3B2
Enzyme 6 Protein Sequence >HSD3B2 protein 
MGWSCLVTGAGGLLGQRIVRLLVEEKELKEIRALDKAFRPELREEFSKLQNRTKLTVLEG
DILDEPFLKRACQDVSVVIHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVFI
YTSSIEVAGPNSYKEIIQNGHEEEPLENTWPTPYPYSKKLAEKAVLAANGWNLKNGDTLY
TCALRPTYIYGEGGPFLSASINEALNNNGILSSVGKFSTVNPVYVGNVAWAHILALRALR
DPKKAPSVRGQFYYISDDTPHQSYDNLNYILSKEFGLRLDSRWSLPLTLMYWIGFLLEVV
SFLLSPIYSYQPPFNRHTVTLSNSVFTFSYKKAQRDLAYKPLYSWEEAKQKTVEWVGSLV
DRHKETLKSKTQ
Enzyme 6 Number of Residues 372
Enzyme 6 Molecular Weight 42053
Enzyme 6 Theoretical pI 8.17
Enzyme 6 GO Classification
Function
  • 3-beta-hydroxy-delta5-steroid dehydrogenase activity
  • catalytic activity
  • intramolecular oxidoreductase activity
  • intramolecular oxidoreductase activity, transposing C=C bonds
  • isomerase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
  • steroid dehydrogenase activity
  • steroid delta-isomerase activity
Process
  • cellular lipid metabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • steroid biosynthesis
  • steroid metabolism
Component
—
Enzyme 6 General Function Cell wall/membrane/envelope biogenesis
Enzyme 6 Specific Function Not Available
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 124297709 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID A2RRA5 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name A2RRA5_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1119 bp 
ATGGGCTGGAGCTGCCTTGTGACAGGAGCAGGAGGGCTTCTGGGTCAGAGGATCGTCCGC
CTGTTGGTGGAAGAGAAGGAACTGAAGGAGATCAGGGCCTTGGACAAGGCCTTCAGACCA
GAATTGAGAGAGGAATTTTCTAAGCTCCAGAACAGGACCAAGCTGACTGTACTTGAAGGA
GACATTCTGGATGAGCCATTCCTGAAAAGAGCCTGCCAGGACGTCTCGGTCGTCATCCAC
ACCGCCTGTATCATTGATGTCTTTGGTGTCACTCACAGAGAGTCCATCATGAATGTCAAT
GTGAAAGGTACCCAGCTACTGTTGGAGGCCTGTGTCCAAGCCAGTGTGCCAGTCTTCATC
TACACCAGTAGCATAGAGGTAGCCGGGCCCAACTCCTACAAGGAAATCATCCAGAACGGC
CACGAAGAAGAGCCTCTGGAAAACACATGGCCCACTCCATACCCGTACAGCAAAAAGCTT
GCTGAGAAGGCTGTGCTGGCGGCTAATGGGTGGAATCTAAAAAATGGTGATACCTTGTAC
ACTTGTGCGTTAAGACCCACATATATCTATGGGGAAGGAGGCCCATTCCTTTCTGCCAGT
ATAAATGAGGCCCTGAACAACAATGGGATCCTGTCAAGTGTTGGAAAGTTCTCTACAGTC
AACCCAGTCTATGTTGGCAACGTGGCCTGGGCCCACATTCTGGCCTTGAGGGCTCTGCGG
GACCCCAAGAAGGCCCCAAGTGTCCGAGGTCAATTCTATTACATCTCAGATGACACGCCT
CACCAAAGCTATGATAACCTTAATTACATCCTGAGCAAAGAGTTTGGCCTCCGCCTTGAT
TCCAGATGGAGCCTTCCTTTAACCCTGATGTACTGGATTGGCTTCCTGCTGGAAGTAGTG
AGCTTCCTACTCAGCCCAATTTACTCCTATCAACCCCCCTTCAACCGCCACACAGTCACA
TTATCAAATAGTGTGTTCACCTTCTCTTACAAGAAGGCTCAGCGAGATCTGGCGTATAAG
CCACTCTACAGCTGGGAGGAAGCCAAGCAGAAAACCGTGGAGTGGGTTGGTTCCCTTGTG
GACCGGCACAAGGAGACCCTGAAGTCCAAGACTCAGTGA
Enzyme 6 GenBank Gene ID BC131488 Link Image
Enzyme 6 GeneCard ID A2RRA5 Link Image
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. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 15062
Enzyme 7 Name Cytochrome P450, family 21, subfamily A, polypeptide 2
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name CYP21A2
Enzyme 7 Protein Sequence >Cytochrome P450, family 21, subfamily A, polypeptide 2 
MLLLGLLLLLPLLAGARLLWNWWKLQSLHLPPLAPGFLHLLQPDLPIYLLGLTQKFGPIY
RLHLGLQDVVVLNSKRTIEEAMVKKWADFAGRPEPLTYKLVSRNYPDLSLGDYSLLWKAH
KKLTRSALLLGIRDSMEPVVEQLTQEFCERMRAQPGTPVAIEEEFSLLTCSIICYLTFGD
KIKDDNLMPAYYKCIQEVLKTWSHWSIQIVDVIPFLRFFPNPGLRRLKQAIEKRDHIVEM
QLRQHKESLVAGQWRDMMDYMLQGVAQPSMEEGSGQLLEGHVHMAAVDLLIGGTETTANT
LSWAVVFLLHHPEIQQRLQEELDHELGPGASSSRVPYKDRARLPLLNATIAEVLRLRPVV
PLALPHRTTRPSSISGYDIPEGTVIIPNLQGAHLDETVWERPHEFWPDRFLEPGKNSRAL
AFGCGARVCLGEPLARLELFVVLTRLLQAFTLLPSGDALPSLQPLPHCSVILKMQPFQVR
LQPRGMGAHSPGQSQ
Enzyme 7 Number of Residues 495
Enzyme 7 Molecular Weight 55974
Enzyme 7 Theoretical pI 7.68
Enzyme 7 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • tetrapyrrole binding
  • transition metal ion binding
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 7 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 7 Specific Function Not Available
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 115528435 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q08AG9 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name Q08AG9_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1488 bp 
ATGCTGCTCCTGGGCCTGCTGCTGCTGCTGCCCCTGCTGGCTGGCGCCCGCCTGCTGTGG
AACTGGTGGAAGCTCCAGAGCCTCCACCTCCCGCCTCTTGCCCCGGGCTTCTTGCACTTG
CTGCAGCCCGACCTCCCAATCTATCTGCTTGGCCTGACTCAGAAATTCGGGCCCATCTAC
AGGCTCCACCTTGGGCTGCAAGATGTGGTGGTGCTGAACTCCAAGAGGACCATTGAGGAA
GCCATGGTCAAAAAGTGGGCAGACTTTGCTGGCAGACCTGAGCCACTTACCTACAAGCTG
GTGTCTAGGAACTACCCGGACCTGTCCTTGGGAGACTACTCCCTGCTCTGGAAAGCCCAC
AAGAAGCTCACCCGCTCAGCCCTGCTGCTGGGCATCCGTGACTCCATGGAGCCAGTGGTG
GAGCAGCTGACCCAGGAGTTCTGTGAGCGCATGAGAGCCCAGCCCGGCACCCCTGTGGCC
ATTGAGGAGGAATTCTCTCTCCTCACCTGCAGCATCATCTGTTACCTCACCTTCGGAGAC
AAGATCAAGGACGACAACTTAATGCCTGCCTATTACAAATGTATCCAGGAGGTGTTAAAA
ACCTGGAGCCACTGGTCCATCCAAATTGTGGACGTGATTCCCTTTCTCAGGTTCTTCCCC
AATCCAGGTCTCCGGAGGCTGAAGCAGGCCATAGAGAAGAGGGATCACATCGTGGAGATG
CAGCTGAGGCAGCACAAGGAGAGCCTCGTGGCAGGCCAGTGGAGGGACATGATGGACTAC
ATGCTCCAAGGGGTGGCGCAGCCGAGCATGGAAGAGGGCTCTGGACAGCTCCTGGAAGGG
CACGTGCACATGGCTGCAGTGGACCTCCTGATCGGTGGCACTGAGACCACAGCAAACACC
CTCTCCTGGGCCGTGGTTTTTTTGCTTCACCACCCTGAGATTCAGCAGCGACTGCAGGAG
GAGCTAGACCACGAACTGGGCCCTGGTGCCTCCAGCTCCCGGGTCCCCTACAAGGACCGT
GCACGGCTGCCCTTGCTCAATGCCACCATCGCCGAGGTGCTGCGCCTGCGGCCCGTTGTG
CCCTTAGCCTTGCCCCACCGCACCACACGGCCCAGCAGCATCTCCGGCTACGACATCCCT
GAGGGCACAGTCATCATTCCGAACCTCCAAGGCGCCCACCTGGATGAGACGGTCTGGGAG
AGGCCACATGAGTTCTGGCCTGATCGCTTCCTGGAGCCAGGCAAGAACTCCAGAGCTCTG
GCCTTCGGCTGCGGTGCCCGCGTGTGCCTGGGCGAGCCGCTGGCGCGCCTGGAGCTCTTC
GTGGTGCTGACCCGACTGCTGCAGGCCTTCACGCTGCTGCCCTCCGGGGACGCCCTGCCC
TCCCTGCAGCCCCTGCCCCACTGCAGTGTCATCCTCAAGATGCAGCCTTTCCAAGTGCGG
CTGCAGCCCCGGGGGATGGGGGCCCACAGCCCGGGCCAGAGCCAGTGA
Enzyme 7 GenBank Gene ID BC125181 Link Image
Enzyme 7 GeneCard ID Q08AG9 Link Image
Enzyme 7 GenAtlas ID CYP21A2 Link Image
Enzyme 7 HGNC ID HGNC:2600 Link Image
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available