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UniProtKB/Swiss-Prot entry P07445


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

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Entry information
Entry name SDIS_PSEPU
Primary accession number P07445
Secondary accession numbers None
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on April 1, 1988 (Sequence version 1)
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
Pseudomonas putida [TaxID: 303] 
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Biotype B;
PubMed=7961420 [NCBI, ExPASy, EBI, Israel, Japan]
Kim S.W., Kim C.Y., Benisek W.F., Choi K.Y.;
"Cloning, nucleotide sequence, and overexpression of the gene coding for delta 5-3-ketosteroid isomerase from Pseudomonas putida biotype B.";
J. Bacteriol. 176:6672-6676(1994).
[2]
PROTEIN SEQUENCE.
STRAIN=Biotype B;
PubMed=3700400 [NCBI, ExPASy, EBI, Israel, Japan]
Linden K.G., Benisek W.F.;
"The amino acid sequence of a delta 5-3-oxosteroid isomerase from Pseudomonas putida biotype B.";
J. Biol. Chem. 261:6454-6460(1986).
[3]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH REACTION INTERMEDIATE ANALOG, AND MUTAGENESIS OF TYR-16 AND ASP-103.
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).
[4]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
DOI=10.1021/bi991040m; PubMed=10529226 [NCBI, ExPASy, EBI, Israel, Japan]
Kim D.-H., Nam G.H., Jang D.S., Choi G., Joo S., Kim J.-S., Oh B.-H., Choi K.-Y.;
"Roles of active site aromatic residues in catalysis by ketosteroid isomerase from Pseudomonas putida biotype B.";
Biochemistry 38:13810-13819(1999).
[5]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT ASN-40/GLU-103 IN COMPLEX WITH REACTION INTERMEDIATE ANALOG, AND MUTAGENESIS OF TYR-16 AND ASP-103.
DOI=10.1021/bi991579k; PubMed=10653633 [NCBI, ExPASy, EBI, Israel, Japan]
Choi G., Ha N.-C., Kim S.W., Kim D.-H., Park S., Oh B.-H., Choi K.-Y.;
"Asp-99 donates a hydrogen bond not to Tyr-14 but to the steroid directly in the catalytic mechanism of delta 5-3-ketosteroid isomerase from Pseudomonas putida biotype B.";
Biochemistry 39:903-909(2000).
[6]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
DOI=10.1074/jbc.M007561200; PubMed=11007792 [NCBI, ExPASy, EBI, Israel, Japan]
Ha N.-C., Kim M.-S., Lee W., Choi K.-Y., Oh B.-H.;
"Detection of large pKa perturbations of an inhibitor and a catalytic group at an enzyme active site, a mechanistic basis for catalytic power of many enzymes.";
J. Biol. Chem. 275:41100-41106(2000).
[7]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT SER-57, AND MUTAGENESIS OF TYR-16 AND TYR-32.
DOI=10.1021/bi015547k; PubMed=11695900 [NCBI, ExPASy, EBI, Israel, Japan]
Nam G.H., Jang D.S., Cha S.-S., Lee T.-H., Kim D.-H., Hong B.H., Yun Y.S., Oh B.-H., Choi K.-Y.;
"Maintenance of alpha-helical structures by phenyl rings in the active-site tyrosine triad contributes to catalysis and stability of ketosteroid isomerase from Pseudomonas putida biotype B.";
Biochemistry 40:13529-13537(2001).
[8]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-92, AND MUTAGENESIS OF LEU-125 AND VAL-127.
DOI=10.1111/j.1742-4658.2005.04627.x; PubMed=15819891 [NCBI, ExPASy, EBI, Israel, Japan]
Yun Y.S., Nam G.H., Kim Y.-G., Oh B.-H., Choi K.-Y.;
"Small exterior hydrophobic cluster contributes to conformational stability and steroid binding in ketosteroid isomerase from Pseudomonas putida biotype B.";
FEBS J. 272:1999-2011(2005).
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
L13127; AAA64437.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A25216; SIPSDP.
3D structure databases
PDB
1C7H; X-ray; 2.50 A; A=1-131.[ExPASy / RCSB / EBI]
1CQS; X-ray; 1.90 A; A/B=1-131.[ExPASy / RCSB / EBI]
1DMM; X-ray; 1.90 A; A=1-131.[ExPASy / RCSB / EBI]
1DMN; X-ray; 2.05 A; A=1-131.[ExPASy / RCSB / EBI]
1DMQ; X-ray; 2.15 A; A=1-131.[ExPASy / RCSB / EBI]
1E3R; X-ray; 2.50 A; A/B=1-131.[ExPASy / RCSB / EBI]
1E3V; X-ray; 2.00 A; A/B=1-131.[ExPASy / RCSB / EBI]
1E97; X-ray; 2.00 A; A=1-131.[ExPASy / RCSB / EBI]
1EA2; X-ray; 1.80 A; A=1-131.[ExPASy / RCSB / EBI]
1GS3; X-ray; 2.10 A; A=1-131.[ExPASy / RCSB / EBI]
1K41; X-ray; 2.20 A; A/B=1-131.[ExPASy / RCSB / EBI]
1OGX; X-ray; 2.00 A; A/B=1-131.[ExPASy / RCSB / EBI]
1OH0; X-ray; 1.10 A; A/B=1-131.[ExPASy / RCSB / EBI]
1OHO; X-ray; 1.90 A; A=1-131.[ExPASy / RCSB / EBI]
1OPY; X-ray; 1.90 A; A=1-131.[ExPASy / RCSB / EBI]
1VZZ; X-ray; 2.30 A; A/B=1-131.[ExPASy / RCSB / EBI]
1W00; X-ray; 2.20 A; A/B=1-131.[ExPASy / RCSB / EBI]
1W01; X-ray; 2.20 A; A/B=1-131.[ExPASy / RCSB / EBI]
1W02; X-ray; 2.30 A; A=1-131.[ExPASy / RCSB / EBI]
1W6Y; X-ray; 2.10 A; A=1-131.[ExPASy / RCSB / EBI]
2INX; X-ray; 1.50 A; A=1-131.[ExPASy / RCSB / EBI]
2PZV; X-ray; 1.25 A; A/B/C/D=1-131.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1C7H; -.
1CQS; -.
1DMM; -.
1DMN; -.
1DMQ; -.
1E3R; -.
1E3V; -.
1E97; -.
1EA2; -.
1GS3; -.
1K41; -.
1OGX; -.
1OH0; -.
1OHO; -.
1OPY; -.
1VZZ; -.
1W00; -.
1W01; -.
1W02; -.
1W6Y; -.
2INX; -.
2PZV; -.
ModBase P07445.
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.
Graphical view of domain structure.
Pfam PF02136; NTF2; 1.
Pfam graphical view of domain structure.
BLOCKS P07445.
ProtoNet P07445.
Other
LinkHub P07445; -.
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   131  131     Steroid Delta-isomerase. PRO_0000097646
ACT_SITE   16    16        Proton donor. 
ACT_SITE   40    40        Proton acceptor. 
BINDING   103   103        Substrate. 
MUTAGEN   16    16        Y->F: Reduces activity 2000-fold. Reduces activity 10000-fold; when associated with E-103; N-103 or L-103. 
MUTAGEN   16    16        Y->S: Reduces activity 20-fold. 
MUTAGEN   32    32        Y->S: Reduces activity 4-fold. 
MUTAGEN   57    57        Y->S: Reduces activity 100-fold. 
MUTAGEN   92    92        W->A: Slightly reduces activity. Reduces protein stability. 
MUTAGEN   103   103        D->A,L: Reduces activity 100-fold. Reduces activity 10000-fold; when associated with F-16. 
MUTAGEN   103   103        D->E: Slightly reduces activity. Reduces activity 10000-fold; when associated with F-16. 
MUTAGEN   103   103        D->N: Reduces activity 4-fold. Reduces activity 10000-fold; when associated with F-16. 
MUTAGEN   125   125        L->A: Slightly reduces activity and reduces protein stability; when associated with A-127. 
MUTAGEN   127   127        V->A: Slightly reduces activity and reduces protein stability; when associated with A-125. 
HELIX   6    22  17      
HELIX   25    31  7      
STRAND   32    41  10      
HELIX   49    61  13      
STRAND   62    64  3      
STRAND   67    72  6      
STRAND   78   107  30      
STRAND   113   119  7      
HELIX   122   124  3      
Sequence information
Length: 131 AA [This is the length of the unprocessed precursor] Molecular weight: 14536 Da [This is the MW of the unprocessed precursor] CRC64: 08711198C13CF014 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNLPTAQEVQ GLMARYIELV DVGDIEAIVQ MYADDATVED PFGQPPIHGR EQIAAFYRQG 

        70         80         90        100        110        120 
LGGGKVRACL TGPVRASHNG CGAMPFRVEM VWNGQPCALD VIDVMRFDEH GRIQTMQAYW 

       130 
SEVNLSVREP Q 

P07445 in FASTA format

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View entry in raw text format (no links)
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