3BHD_COMTE
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 03-AUG-2022, entry version 119.
DE RecName: Full=3-beta-hydroxysteroid dehydrogenase;
DE EC=1.1.1.51;
OS Comamonas testosteroni (Pseudomonas testosteroni).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=285;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 11996 / DSM 50244 / IAM 12419 / JCM 5832 / NCIMB 8955 / NBRC
RC 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 / IAM 12419 / JCM 5832 / NCIMB 8955 / NBRC
RC 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 / IAM 12419 / JCM 5832 / NCIMB 8955 / NBRC
RC 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 (1.22 ANGSTROMS).
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=NAD(+) + testosterone = androst-4-ene-3,17-dione + H(+) +
CC NADH; 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=NADP(+) + testosterone = androst-4-ene-3,17-dione + H(+) +
CC NADPH; 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 -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/STDH/";
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DR EMBL; X63379; CAA44977.1; -; Genomic_DNA.
DR EMBL; U41265; AAA25742.1; -; Genomic_DNA.
DR PIR; S48129; S48129.
DR RefSeq; WP_003080542.1; NZ_UFXL01000001.1.
DR PDB; 1HXH; X-ray; 1.22 A; A/B/C/D=2-254.
DR PDBsum; 1HXH; -.
DR AlphaFoldDB; P19871; -.
DR SMR; P19871; -.
DR GeneID; 63999690; -.
DR BioCyc; MetaCyc:MON-16923; -.
DR BRENDA; 1.1.1.51; 1590.
DR EvolutionaryTrace; P19871; -.
DR GO; GO:0035410; F:dihydrotestosterone 17-beta-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0047045; F:testosterone 17-beta-dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0047035; F:testosterone dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 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..112
FT /evidence="ECO:0007829|PDB:1HXH"
FT HELIX 114..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
