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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
 
 
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