ID 3BHD_COMTE Reviewed; 254 AA. AC P19871; Q52587; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 5. DT 04-NOV-2026, entry version 132. DE RecName: Full=3-beta-hydroxysteroid dehydrogenase; DE EC=1.1.1.51; OS Comamonas testosteroni (Pseudomonas testosteroni). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Comamonadaceae; Comamonas. OX NCBI_TaxID=285; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 11996 / DSM 50244 / CCUG 1426 / IAM 12419 / JCM 5832 / RC NCIMB 8955 / NBRC 14951 / NCTC 10698 / NRRL B-2611; RX PubMed=8382516; DOI=10.1016/0960-0760(93)90020-w; RA Abalain J.H., di Stefano S., Amet Y., Quemener E., Abalain-Colloc M.L., RA Floch H.H.; RT "Cloning, DNA sequencing and expression of (3-17)beta hydroxysteroid RT dehydrogenase from Pseudomonas testosteroni."; RL J. Steroid Biochem. Mol. Biol. 44:133-139(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 11996 / DSM 50244 / CCUG 1426 / IAM 12419 / JCM 5832 / RC NCIMB 8955 / NBRC 14951 / NCTC 10698 / NRRL B-2611; RX PubMed=15026087; DOI=10.1016/j.jsbmb.2003.10.010; RA Pruneda-Paz J.L., Linares M., Cabrera J.E., Genti-Raimondi S.; RT "Identification of a novel steroid inducible gene associated with the beta RT hsd locus of Comamonas testosteroni."; RL J. Steroid Biochem. Mol. Biol. 88:91-100(2004). RN [3] RP PROTEIN SEQUENCE OF 2-254. RX PubMed=2026158; DOI=10.1111/j.1432-1033.1991.tb15919.x; RA Yin S.-J., Vagelopoulos N., Lundquist G., Joernvall H.; RT "Pseudomonas 3 beta-hydroxysteroid dehydrogenase. Primary structure and RT relationships to other steroid dehydrogenases."; RL Eur. J. Biochem. 197:359-365(1991). RN [4] RP CRYSTALLIZATION, AND SUBUNIT. RC STRAIN=ATCC 11996 / DSM 50244 / CCUG 1426 / IAM 12419 / JCM 5832 / RC NCIMB 8955 / NBRC 14951 / NCTC 10698 / NRRL B-2611; RX PubMed=8617258; DOI=10.1111/j.1432-1033.1996.t01-1-00144.x; RA Benach J., Knapp S., Oppermann U.C.T., Haegllund O., Joernvall H., RA Ladenstein R.; RT "Crystallization and crystal packing of recombinant 3 (or 17) beta- RT hydroxysteroid dehydrogenase from Comamonas testosteroni ATTC 11996."; RL Eur. J. Biochem. 236:144-148(1996). RN [5] RP X-RAY CRYSTALLOGRAPHY. RX PubMed=12475215; DOI=10.1021/bi0203684; RA Benach J., Filling C., Oppermann U.C.T., Roversi P., Bricogne G., RA Berndt K.D., Joernvall H., Ladenstein R.; RT "Structure of bacterial 3beta/17beta-hydroxysteroid dehydrogenase at 1.2 A RT resolution: a model for multiple steroid recognition."; RL Biochemistry 41:14659-14668(2002). CC -!- CATALYTIC ACTIVITY: CC Reaction=testosterone + NAD(+) = androst-4-ene-3,17-dione + NADH + CC H(+); Xref=Rhea:RHEA:14929, ChEBI:CHEBI:15378, ChEBI:CHEBI:16422, CC ChEBI:CHEBI:17347, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.51; CC -!- CATALYTIC ACTIVITY: CC Reaction=testosterone + NADP(+) = androst-4-ene-3,17-dione + NADPH + CC H(+); Xref=Rhea:RHEA:14981, ChEBI:CHEBI:15378, ChEBI:CHEBI:16422, CC ChEBI:CHEBI:17347, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.51; CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:8617258}. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X63379; CAA44977.1; -; Genomic_DNA. DR EMBL; U41265; AAA25742.1; -; Genomic_DNA. DR PIR; S48129; S48129. DR RefSeq; WP_003080542.1; NZ_BBJZ01000009.1. DR PDB; 1HXH; X-ray; 1.22 A; A/B/C/D=2-254. DR AlphaFoldDB; P19871; -. DR SMR; P19871; -. DR GeneID; 63999690; -. DR BioCyc; MetaCyc:MONOMER-16923; -. DR BRENDA; 1.1.1.51; 1590. DR EvolutionaryTrace; P19871; -. DR GO; GO:0047035; F:testosterone dehydrogenase (NAD+) activity; IEA:RHEA. DR GO; GO:0047045; F:testosterone dehydrogenase (NADP+) activity; IEA:RHEA. DR CDD; cd05341; 3beta-17beta-HSD_like_SDR_c; 1. DR FunFam; 3.40.50.720:FF:000084; Short-chain dehydrogenase reductase; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR43180; 3-OXOACYL-(ACYL-CARRIER-PROTEIN) REDUCTASE (AFU_ORTHOLOGUE AFUA_6G11210); 1. DR PANTHER; PTHR43180:SF28; NAD(P)-BINDING ROSSMANN-FOLD SUPERFAMILY PROTEIN; 1. DR Pfam; PF13561; adh_short_C2; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Lipid metabolism; NAD; KW Oxidoreductase; Steroid metabolism. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2026158" FT CHAIN 2..254 FT /note="3-beta-hydroxysteroid dehydrogenase" FT /id="PRO_0000054446" FT ACT_SITE 152 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001" FT BINDING 12..40 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 61 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 139 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 156 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT CONFLICT 14..15 FT /note="GG -> VV (in Ref. 1; CAA44977)" FT /evidence="ECO:0000305" FT CONFLICT 41 FT /note="Missing (in Ref. 1; CAA44977)" FT /evidence="ECO:0000305" FT CONFLICT 178 FT /note="R -> RR (in Ref. 1; CAA44977)" FT /evidence="ECO:0000305" FT CONFLICT 241 FT /note="S -> G (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT TURN 4..7 FT /evidence="ECO:0007829|PDB:1HXH" FT STRAND 9..12 FT /evidence="ECO:0007829|PDB:1HXH" FT TURN 13..16 FT /evidence="ECO:0007829|PDB:1HXH" FT HELIX 18..29 FT /evidence="ECO:0007829|PDB:1HXH" FT STRAND 33..37 FT /evidence="ECO:0007829|PDB:1HXH" FT HELIX 41..51 FT /evidence="ECO:0007829|PDB:1HXH" FT STRAND 55..58 FT /evidence="ECO:0007829|PDB:1HXH" FT HELIX 65..79 FT /evidence="ECO:0007829|PDB:1HXH" FT STRAND 84..87 FT /evidence="ECO:0007829|PDB:1HXH" FT TURN 97..99 FT /evidence="ECO:0007829|PDB:1HXH" FT HELIX 102..108 FT /evidence="ECO:0007829|PDB:1HXH" FT HELIX 109..114 FT /evidence="ECO:0007829|PDB:1HXH" FT HELIX 115..127 FT /evidence="ECO:0007829|PDB:1HXH" FT TURN 128..130 FT /evidence="ECO:0007829|PDB:1HXH" FT STRAND 132..137 FT /evidence="ECO:0007829|PDB:1HXH" FT HELIX 140..142 FT /evidence="ECO:0007829|PDB:1HXH" FT HELIX 150..173 FT /evidence="ECO:0007829|PDB:1HXH" FT STRAND 177..187 FT /evidence="ECO:0007829|PDB:1HXH" FT HELIX 190..195 FT /evidence="ECO:0007829|PDB:1HXH" FT HELIX 202..205 FT /evidence="ECO:0007829|PDB:1HXH" FT TURN 209..211 FT /evidence="ECO:0007829|PDB:1HXH" FT HELIX 220..231 FT /evidence="ECO:0007829|PDB:1HXH" FT HELIX 233..235 FT /evidence="ECO:0007829|PDB:1HXH" FT STRAND 242..248 FT /evidence="ECO:0007829|PDB:1HXH" FT TURN 250..253 FT /evidence="ECO:0007829|PDB:1HXH" SQ SEQUENCE 254 AA; 26952 MW; FB6EC90B151975DB CRC64; MTNRLQGKVA LVTGGASGVG LEVVKLLLGE GAKVAFSDIN EAAGQQLAAE LGERSMFVRH DVSSEADWTL VMAAVQRRLG TLNVLVNNAG ILLPGDMETG RLEDFSRLLK INTESVFIGC QQGIAAMKET GGSIINMASV SSWLPIEQYA GYSASKAAVS ALTRAAALSC RKQGYAIRVN SIHPDGIYTP MMQASLPKGV SKEMVLHDPK LNRAGRAYMP ERIAQLVLFL ASDESSVMSG SELHADNSIL GMGL //