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UniProtKB/Swiss-Prot entry P00947


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SDIS_COMTE
Primary accession number P00947
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on February 1, 1991 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 68)
Name and origin of the protein
Protein name Steroid Delta-isomerase
Synonyms EC 5.3.3.1
Delta(5)-3-ketosteroid isomerase
Gene name
Name: ksi
From
Comamonas testosteroni (Pseudomonas testosteroni) [TaxID: 285] 
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Comamonadaceae; Comamonas.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(88)90384-8; PubMed=3224818 [NCBI, ExPASy, EBI, Israel, Japan]
Choi K.Y., Benisek W.F.;
"Nucleotide sequence of the gene for the delta 5-3-ketosteroid isomerase of Pseudomonas testosteroni.";
Gene 69:121-129(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3480517 [NCBI, ExPASy, EBI, Israel, Japan]
Kuliopulos A., Shortle D., Talalay P.;
"Isolation and sequencing of the gene encoding delta 5-3-ketosteroid isomerase of Pseudomonas testosteroni: overexpression of the protein.";
Proc. Natl. Acad. Sci. U.S.A. 84:8893-8897(1987).
[3]
PRELIMINARY PROTEIN SEQUENCE.
PubMed=5135313 [NCBI, ExPASy, EBI, Israel, Japan]
Benson A.M., Jarabak R., Talalay P.;
"The amino acid sequence of delta 5-3-ketosteroid isomerase of Pseudomonas testosteroni.";
J. Biol. Chem. 246:7514-7525(1971).
[4]
CHARACTERIZATION.
DOI=10.1016/0014-5793(73)80431-4; PubMed=4753764 [NCBI, ExPASy, EBI, Israel, Japan]
Weintraub H., Vincent F., Baulieu E.-E., Alfsen A.;
"Molecular weight determination and structural studies of Pseudomonas testosteroni delta 5 leads to 4-3-oxosteroid isomerase (EC 5.3.3.1).";
FEBS Lett. 37:82-88(1973).
[5]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
DOI=10.1021/bi971546+; PubMed=9369474 [NCBI, ExPASy, EBI, Israel, Japan]
Kim S.-W., Cha S.-S., Cho H.-S., Kim J.-S., Ha N.-C., Cho M.-J., Joo S., Kim K.-K., Choi K.-Y., Oh B.-H.;
"High-resolution crystal structures of delta5-3-ketosteroid isomerase with and without a reaction intermediate analogue.";
Biochemistry 36:14030-14036(1997).
[6]
STRUCTURE BY NMR, AND MUTAGENESIS OF ASP-99.
DOI=10.1126/science.276.5311.415; PubMed=9103200 [NCBI, ExPASy, EBI, Israel, Japan]
Wu Z.R., Ebrahimian S., Zawrotny M.E., Thornburg L.D., Perez-Alvarado G.C., Brothers P., Pollack R.M., Summers M.F.;
"Solution structure of 3-oxo-delta5-steroid isomerase.";
Science 276:415-418(1997).
[7]
STRUCTURE BY NMR IN COMPLEX WITH PRODUCT ANALOG.
DOI=10.1021/bi981447b; PubMed=9778345 [NCBI, ExPASy, EBI, Israel, Japan]
Massiah M.A., Abeygunawardana C., Gittis A.G., Mildvan A.S.;
"Solution structure of delta 5-3-ketosteroid isomerase complexed with the steroid 19-nortestosterone hemisuccinate.";
Biochemistry 37:14701-14712(1998).
[8]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH REACTION INTERMEDIATE ANALOG.
DOI=10.1074/jbc.274.46.32863; PubMed=10551849 [NCBI, ExPASy, EBI, Israel, Japan]
Cho H.-S., Ha N.-C., Choi G., Kim H.-J., Lee D., Oh K.S., Kim K.S., Lee W., Choi K.Y., Oh B.-H.;
"Crystal structure of delta(5)-3-ketosteroid isomerase from Pseudomonas testosteroni in complex with equilenin settles the correct hydrogen bonding scheme for transition state stabilization.";
J. Biol. Chem. 274:32863-32868(1999).
[9]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT ALA-39 IN COMPLEX WITH REACTION INTERMEDIATE ANALOG.
DOI=10.1042/BJ20030263; PubMed=12852789 [NCBI, ExPASy, EBI, Israel, Japan]
Nam G.H., Cha S.-S., Yun Y.S., Oh Y.H., Hong B.H., Lee H.-S., Choi K.-Y.;
"The conserved cis-Pro39 residue plays a crucial role in the proper positioning of the catalytic base Asp38 in ketosteroid isomerase from Comamonas testosteroni.";
Biochem. J. 375:297-305(2003).
[10]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT TRP-116.
DOI=10.1074/jbc.M302166200; PubMed=12734184 [NCBI, ExPASy, EBI, Israel, Japan]
Yun Y.S., Lee T.-H., Nam G.H., Jang do S., Shin S., Oh B.-H., Choi K.-Y.;
"Origin of the different pH activity profile in two homologous ketosteroid isomerases.";
J. Biol. Chem. 278:28229-28236(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M22749; AAA25872.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J03568; AAA25871.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JT0336; SIPSDT.
3D structure databases
PDB
1BUQ; NMR; -; A/B=1-125.[ExPASy / RCSB / EBI]
1ISK; NMR; -; A/B=1-125.[ExPASy / RCSB / EBI]
1OCV; X-ray; 2.00 A; A/B/C/D=1-125.[ExPASy / RCSB / EBI]
1OGZ; X-ray; 2.30 A; A=1-125.[ExPASy / RCSB / EBI]
1OHP; X-ray; 1.53 A; A/B/C/D=1-125.[ExPASy / RCSB / EBI]
1OHS; X-ray; 1.70 A; A/B/C/D=1-125.[ExPASy / RCSB / EBI]
1QJG; X-ray; 2.30 A; A/B/C/D/E/F=1-125.[ExPASy / RCSB / EBI]
8CHO; X-ray; 2.30 A; A=1-125.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BUQ; -.
1ISK; -.
1OCV; -.
1OGZ; -.
1OHP; -.
1OHS; -.
1QJG; -.
8CHO; -.
ModBase P00947.
Ontologies
GO
GO:0004769; Molecular function: steroid delta-isomerase activity (inferred from electronic annotation from EC).
GO:0008202; Biological process: steroid metabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002075; NTF2.
IPR011944; Steroid_delta5-4_isomerase.
Graphical view of domain structure.
Pfam PF02136; NTF2; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR02246; CHP2246; 1.
BLOCKS P00947.
ProtoNet P00947.
Other
LinkHub P00947; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Isomerase; Lipid metabolism; Steroid metabolism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   125  125     Steroid Delta-isomerase. PRO_0000097644
ACT_SITE   14    14        Proton donor. 
ACT_SITE   38    38        Proton acceptor. 
BINDING   99    99        Substrate. 
MUTAGEN   39    39        P->A: Perturbs active site geometry and lowers activity. 
MUTAGEN   99    99        D->A: Lowers activity 3000-fold. 
MUTAGEN   116   116        F->W: Slightly lower activity at neutral pH. Increased catalytic activity at pH 3.8. 
HELIX   4    20  17      
HELIX   23    27  5      
STRAND   30    39  10      
STRAND   45    47  3      
HELIX   48    58  11      
STRAND   64    67  4      
STRAND   72    74  3      
STRAND   77    87  11      
STRAND   92    95  4      
STRAND   98   103  6      
STRAND   109   115  7      
HELIX   118   120  3      
STRAND   121   123  3      
Sequence information
Length: 125 AA [This is the length of the unprocessed precursor] Molecular weight: 13398 Da [This is the MW of the unprocessed precursor] CRC64: 2ECD410D4B929430 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNTPEHMTAV VQRYVAALNA GDLDGIVALF ADDATVEDPV GSEPRSGTAA IREFYANSLK 

        70         80         90        100        110        120 
LPLAVELTQE VRAVANEAAF AFTVSFEYQG RKTVVAPIDH FRFNGAGKVV SMRALFGEKN 


IHAGA 

P00947 in FASTA format

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