SDIS_COMTE
ID SDIS_COMTE Reviewed; 125 AA.
AC P00947;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Steroid Delta-isomerase;
DE EC=5.3.3.1;
DE AltName: Full=Delta(5)-3-ketosteroid isomerase;
GN Name=ksi;
OS Comamonas testosteroni (Pseudomonas testosteroni).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=285;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3224818; DOI=10.1016/0378-1119(88)90384-8;
RA Choi K.Y., Benisek W.F.;
RT "Nucleotide sequence of the gene for the delta 5-3-ketosteroid isomerase of
RT Pseudomonas testosteroni.";
RL Gene 69:121-129(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3480517; DOI=10.1073/pnas.84.24.8893;
RA Kuliopulos A., Shortle D., Talalay P.;
RT "Isolation and sequencing of the gene encoding delta 5-3-ketosteroid
RT isomerase of Pseudomonas testosteroni: overexpression of the protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:8893-8897(1987).
RN [3]
RP PRELIMINARY PROTEIN SEQUENCE.
RX PubMed=5135313; DOI=10.1016/s0021-9258(19)45806-7;
RA Benson A.M., Jarabak R., Talalay P.;
RT "The amino acid sequence of delta 5-3-ketosteroid isomerase of Pseudomonas
RT testosteroni.";
RL J. Biol. Chem. 246:7514-7525(1971).
RN [4]
RP CHARACTERIZATION.
RX PubMed=4753764; DOI=10.1016/0014-5793(73)80431-4;
RA Weintraub H., Vincent F., Baulieu E.-E., Alfsen A.;
RT "Molecular weight determination and structural studies of Pseudomonas
RT testosteroni delta 5 leads to 4-3-oxosteroid isomerase (EC 5.3.3.1).";
RL FEBS Lett. 37:82-88(1973).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=9369474; DOI=10.1021/bi971546+;
RA Kim S.-W., Cha S.-S., Cho H.-S., Kim J.-S., Ha N.-C., Cho M.-J., Joo S.,
RA Kim K.-K., Choi K.-Y., Oh B.-H.;
RT "High-resolution crystal structures of delta5-3-ketosteroid isomerase with
RT and without a reaction intermediate analogue.";
RL Biochemistry 36:14030-14036(1997).
RN [6]
RP STRUCTURE BY NMR, AND MUTAGENESIS OF ASP-99.
RX PubMed=9103200; DOI=10.1126/science.276.5311.415;
RA Wu Z.R., Ebrahimian S., Zawrotny M.E., Thornburg L.D., Perez-Alvarado G.C.,
RA Brothers P., Pollack R.M., Summers M.F.;
RT "Solution structure of 3-oxo-delta5-steroid isomerase.";
RL Science 276:415-418(1997).
RN [7]
RP STRUCTURE BY NMR IN COMPLEX WITH PRODUCT ANALOG.
RX PubMed=9778345; DOI=10.1021/bi981447b;
RA Massiah M.A., Abeygunawardana C., Gittis A.G., Mildvan A.S.;
RT "Solution structure of delta 5-3-ketosteroid isomerase complexed with the
RT steroid 19-nortestosterone hemisuccinate.";
RL Biochemistry 37:14701-14712(1998).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH REACTION INTERMEDIATE
RP ANALOG.
RX PubMed=10551849; DOI=10.1074/jbc.274.46.32863;
RA Cho H.-S., Ha N.-C., Choi G., Kim H.-J., Lee D., Oh K.S., Kim K.S., Lee W.,
RA Choi K.Y., Oh B.-H.;
RT "Crystal structure of delta(5)-3-ketosteroid isomerase from Pseudomonas
RT testosteroni in complex with equilenin settles the correct hydrogen bonding
RT scheme for transition state stabilization.";
RL J. Biol. Chem. 274:32863-32868(1999).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT ALA-39 IN COMPLEX WITH
RP REACTION INTERMEDIATE ANALOG.
RX PubMed=12852789; DOI=10.1042/bj20030263;
RA Nam G.H., Cha S.-S., Yun Y.S., Oh Y.H., Hong B.H., Lee H.-S., Choi K.-Y.;
RT "The conserved cis-Pro39 residue plays a crucial role in the proper
RT positioning of the catalytic base Asp38 in ketosteroid isomerase from
RT Comamonas testosteroni.";
RL Biochem. J. 375:297-305(2003).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT TRP-116.
RX PubMed=12734184; DOI=10.1074/jbc.m302166200;
RA Yun Y.S., Lee T.-H., Nam G.H., Jang do S., Shin S., Oh B.-H., Choi K.-Y.;
RT "Origin of the different pH activity profile in two homologous ketosteroid
RT isomerases.";
RL J. Biol. Chem. 278:28229-28236(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid;
CC Xref=Rhea:RHEA:14709, ChEBI:CHEBI:47907, ChEBI:CHEBI:47909;
CC EC=5.3.3.1;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10551849,
CC ECO:0000269|PubMed:12852789, ECO:0000269|PubMed:9778345}.
CC -!- INDUCTION: By steroids.
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DR EMBL; M22749; AAA25872.1; -; Genomic_DNA.
DR EMBL; J03568; AAA25871.1; -; Genomic_DNA.
DR PIR; JT0336; SIPSDT.
DR RefSeq; WP_003078309.1; NZ_UFXL01000001.1.
DR PDB; 1BUQ; NMR; -; A/B=1-125.
DR PDB; 1ISK; NMR; -; A/B=1-125.
DR PDB; 1OCV; X-ray; 2.00 A; A/B/C/D=1-125.
DR PDB; 1OGZ; X-ray; 2.30 A; A=1-125.
DR PDB; 1OHP; X-ray; 1.53 A; A/B/C/D=1-125.
DR PDB; 1OHS; X-ray; 1.70 A; A/B/C/D=1-125.
DR PDB; 1QJG; X-ray; 2.30 A; A/B/C/D/E/F=1-125.
DR PDB; 3M8C; X-ray; 2.10 A; A/B/C/D=1-125.
DR PDB; 3MHE; X-ray; 1.72 A; A/B=1-125.
DR PDB; 3MKI; X-ray; 2.00 A; A/B/C/D=1-125.
DR PDB; 3MYT; X-ray; 1.96 A; A/B/C/D=1-125.
DR PDB; 3NBR; X-ray; 1.73 A; A=1-125.
DR PDB; 3NHX; X-ray; 1.59 A; A=1-125.
DR PDB; 3NM2; X-ray; 1.89 A; A=1-125.
DR PDB; 3NUV; X-ray; 1.76 A; A/B=1-125.
DR PDB; 3NXJ; X-ray; 1.97 A; A/B=1-125.
DR PDB; 3OV4; X-ray; 1.83 A; A/B/C/D=1-125.
DR PDB; 3T8U; X-ray; 2.50 A; A/B/C/D=1-125.
DR PDB; 3UNL; X-ray; 2.52 A; A/B/C/D=1-125.
DR PDB; 4L7K; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/O=1-125.
DR PDB; 5DRE; X-ray; 2.15 A; A=1-125.
DR PDB; 5UGI; X-ray; 1.80 A; A=1-125.
DR PDB; 6UAD; X-ray; 1.75 A; A=1-125.
DR PDB; 6UAE; X-ray; 1.93 A; A/B/C/D=1-125.
DR PDB; 8CHO; X-ray; 2.30 A; A=1-125.
DR PDBsum; 1BUQ; -.
DR PDBsum; 1ISK; -.
DR PDBsum; 1OCV; -.
DR PDBsum; 1OGZ; -.
DR PDBsum; 1OHP; -.
DR PDBsum; 1OHS; -.
DR PDBsum; 1QJG; -.
DR PDBsum; 3M8C; -.
DR PDBsum; 3MHE; -.
DR PDBsum; 3MKI; -.
DR PDBsum; 3MYT; -.
DR PDBsum; 3NBR; -.
DR PDBsum; 3NHX; -.
DR PDBsum; 3NM2; -.
DR PDBsum; 3NUV; -.
DR PDBsum; 3NXJ; -.
DR PDBsum; 3OV4; -.
DR PDBsum; 3T8U; -.
DR PDBsum; 3UNL; -.
DR PDBsum; 4L7K; -.
DR PDBsum; 5DRE; -.
DR PDBsum; 5UGI; -.
DR PDBsum; 6UAD; -.
DR PDBsum; 6UAE; -.
DR PDBsum; 8CHO; -.
DR AlphaFoldDB; P00947; -.
DR BMRB; P00947; -.
DR SMR; P00947; -.
DR DrugBank; DB01561; Androstanedione.
DR DrugBank; DB03515; Equilenin.
DR DrugBank; DB04693; Estrane-3,17-dione.
DR DrugBank; DB08308; SUCCINIC ACID MONO-(13-METHYL-3-OXO-2,3,6,7,8,9,10,11,12,13,14,15,16,17-TETRADECAHYDRO-1H-CYCLOPENTA[A]PHENANTHREN-17-YL) ESTER.
DR GeneID; 64000200; -.
DR KEGG; ag:AAA25872; -.
DR BRENDA; 5.3.3.1; 1590.
DR SABIO-RK; P00947; -.
DR EvolutionaryTrace; P00947; -.
DR GO; GO:0004769; F:steroid delta-isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00781; ketosteroid_isomerase; 1.
DR InterPro; IPR039256; Ketosteroid_isomerase.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR002075; NTF2_dom.
DR InterPro; IPR011944; Steroid_delta5-4_isomerase.
DR Pfam; PF02136; NTF2; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR TIGRFAMs; TIGR02246; TIGR02246; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Isomerase; Lipid metabolism;
KW Steroid metabolism.
FT CHAIN 1..125
FT /note="Steroid Delta-isomerase"
FT /id="PRO_0000097644"
FT ACT_SITE 14
FT /note="Proton donor"
FT ACT_SITE 38
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:3480517"
FT BINDING 99
FT /ligand="substrate"
FT MUTAGEN 39
FT /note="P->A: Perturbs active site geometry and lowers
FT activity."
FT MUTAGEN 99
FT /note="D->A: Lowers activity 3000-fold."
FT /evidence="ECO:0000269|PubMed:9103200"
FT MUTAGEN 116
FT /note="F->W: Slightly lower activity at neutral pH.
FT Increased catalytic activity at pH 3.8."
FT HELIX 4..20
FT /evidence="ECO:0007829|PDB:1OHP"
FT HELIX 23..27
FT /evidence="ECO:0007829|PDB:1OHP"
FT STRAND 30..39
FT /evidence="ECO:0007829|PDB:1OHP"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1OHP"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:1OHP"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1OHP"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1OHP"
FT STRAND 77..88
FT /evidence="ECO:0007829|PDB:1OHP"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:1OHP"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:1OHP"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:1ISK"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:1OHP"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1OHP"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1OHP"
SQ SEQUENCE 125 AA; 13398 MW; 2ECD410D4B929430 CRC64;
MNTPEHMTAV VQRYVAALNA GDLDGIVALF ADDATVEDPV GSEPRSGTAA IREFYANSLK
LPLAVELTQE VRAVANEAAF AFTVSFEYQG RKTVVAPIDH FRFNGAGKVV SMRALFGEKN
IHAGA
