OASD_COMTE
ID OASD_COMTE Reviewed; 530 AA.
AC Q59327;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase;
DE EC=1.3.99.5;
DE AltName: Full=Delta 4, 5-alpha steroid dehydrogenase;
OS Comamonas testosteroni (Pseudomonas testosteroni).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=285;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A DEHYDROGENASE, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, COFACTOR, AND SUBSTRATE SPECIFICITY.
RX PubMed=8655514; DOI=10.1128/jb.178.11.3322-3330.1996;
RA Florin C., Kohler T., Grandguillot M., Plesiat P.;
RT "Comamonas testosteroni 3-ketosteroid-delta 4(5 alpha)-dehydrogenase: gene
RT and protein characterization.";
RL J. Bacteriol. 178:3322-3330(1996).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=13673006; DOI=10.1016/s0021-9258(18)69859-x;
RA Levy H.R., Talalay P.;
RT "Bacterial oxidation of steroids. II. Studies on the enzymatic mechanism of
RT ring A dehydrogenation.";
RL J. Biol. Chem. 234:2014-2021(1959).
CC -!- FUNCTION: Involved in the degradation of steroids having an A:B ring
CC fusion in a trans configuration. Catalyzes the elimination of hydrogens
CC located at positions 4 and 5 and the introduction of double bonds into
CC ring A. {ECO:0000269|PubMed:8655514}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + a 3-oxo-5alpha-steroid = a 3-oxo-Delta(4)-steroid + AH2;
CC Xref=Rhea:RHEA:13805, ChEBI:CHEBI:13193, ChEBI:CHEBI:13601,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:47909; EC=1.3.99.5;
CC Evidence={ECO:0000269|PubMed:8655514};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-androstan-3,17-dione + A = AH2 + androst-4-ene-3,17-
CC dione; Xref=Rhea:RHEA:51048, ChEBI:CHEBI:13193, ChEBI:CHEBI:15994,
CC ChEBI:CHEBI:16422, ChEBI:CHEBI:17499; EC=1.3.99.5;
CC Evidence={ECO:0000269|PubMed:8655514};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-androst-1-ene-3,17-dione + A = AH2 + androsta-1,4-
CC diene-3,17-dione; Xref=Rhea:RHEA:51060, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:40799, ChEBI:CHEBI:133930;
CC EC=1.3.99.5; Evidence={ECO:0000269|PubMed:8655514};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000305|PubMed:8655514};
CC -!- ACTIVITY REGULATION: Inhibition occurs with substrate concentrations
CC above 25 uM. {ECO:0000269|PubMed:8655514}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.6 uM for 5-alpha-1-androstene-3,17-dione (at 30 degrees Celsius
CC and at pH 8.2) {ECO:0000269|PubMed:8655514};
CC KM=16.1 uM for 5-alpha-androstane-3,17-dione (at 30 degrees Celsius
CC and at pH 8.2) {ECO:0000269|PubMed:8655514};
CC Vmax=456 nmol/min/mg enzyme with 5-alpha-androstane-3,17-dione as
CC substrate (at 30 degrees Celsius and at pH 8.2)
CC {ECO:0000269|PubMed:8655514};
CC Vmax=700 nmol/min/mg enzyme with 5-alpha-1-androstene-3,17-dione as
CC substrate (at 30 degrees Celsius and at pH 8.2)
CC {ECO:0000269|PubMed:8655514};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:8655514};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:8655514};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC {ECO:0000305}.
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DR EMBL; L23428; AAB08517.1; -; Genomic_DNA.
DR PIR; JC6030; JC6030.
DR AlphaFoldDB; Q59327; -.
DR SMR; Q59327; -.
DR KEGG; ag:AAB08517; -.
DR BioCyc; MetaCyc:MON-16925; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0047571; F:3-oxosteroid 1-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0006706; P:steroid catabolic process; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
DR Gene3D; 3.90.700.10; -; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR Pfam; PF00890; FAD_binding_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF56425; SSF56425; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Lipid metabolism; Membrane; Oxidoreductase;
KW Steroid metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..530
FT /note="3-oxo-5-alpha-steroid 4-dehydrogenase"
FT /id="PRO_0000418533"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 33..62
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 530 AA; 57289 MW; 5E5D6CEAC0BF2EC1 CRC64;
MSNVKKHVST INPVGEVLDV GSADEVQWSD ASDVVVVGWG GAGASAAIEA REQGAEVLVI
ERFSGGGASV LSGGVVYAGA VPATRRKPAS RFTEAMTAYL KHEVNGVVSD ETLARFSRDS
VTNLNWLEKQ GATFASTMPG YKTSYPADGM YLYYSGNEVV PAYGNPQLLK KPPPRGHRVV
AKGQSGAMFF AALQKSTLAH GARTLTQARV QRLVREKDSG RVLGVEVMVL PEGDPRTERH
KKLDELVAKS ACIRRRVPRR VAVNVRRSRA RSARSATSVP AKVWCCPLAA ISSIRNCWSM
RRYKPGWLTG AAGCDGSGLR LGQSVGGIAQ DLNNISAWRF ITPPSVWPKG LVVNIQGERF
CNEQVYGAKL GYEMMEKQGG QAWLIIDSNV RRQAAWQCLF GGLWAFQSMP ALALMYKVAI
KGKSVDDLAK KLRMDAAVLQ LQFDRANAPA RGEIEDPLGK SQDMRHEFKG GSLFAIDISI
SQKMFPLAVL SLGGLKVNED NGAVIDGAGY DIPGLYAAGV PPLVWLPRVT
