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Reviewed, UniProtKB/Swiss-Prot P00947 (SDIS_COMTE)

Last modified June 16, 2009. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Steroid Delta-isomerase
    EC=5.3.3.1
Alternative name(s):
    Delta(5)-3-ketosteroid isomerase
Gene names
Name: ksi
OrganismComamonas testosteroni (Pseudomonas testosteroni)
Taxonomic identifier285 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeComamonas

Protein attributes

Sequence length125 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid.

Subunit structure

Homodimer.

Induction

By steroids.

Ontologies

Keywords
   Biological processLipid metabolism
Steroid metabolism
   Molecular functionIsomerase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processsteroid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

transport

Inferred from electronic annotation. Source: InterPro

   Cellular componentintracellular

Inferred from electronic annotation. Source: InterPro

   Molecular functionsteroid delta-isomerase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 125125Steroid Delta-isomerase
PRO_0000097644

Sites

Active site141Proton donor
Active site381Proton acceptor Ref.2
Binding site991Substrate

Experimental info

Mutagenesis391P → A: Perturbs active site geometry and lowers activity.
Mutagenesis991D → A: Lowers activity 3000-fold. Ref.6
Mutagenesis1161F → W: Slightly lower activity at neutral pH. Increased catalytic activity at pH 3.8.

Secondary structure

......................... 125
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00947-1 [UniParc].

Last modified February 1, 1991. Version 2.
Checksum: 2ECD410D4B929430

FASTA12513,398
        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 

« Hide

References

[1]"Nucleotide sequence of the gene for the delta 5-3-ketosteroid isomerase of Pseudomonas testosteroni."
Choi K.Y., Benisek W.F.
Gene 69:121-129(1988) [PubMed: 3224818] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Isolation and sequencing of the gene encoding delta 5-3-ketosteroid isomerase of Pseudomonas testosteroni: overexpression of the protein."
Kuliopulos A., Shortle D., Talalay P.
Proc. Natl. Acad. Sci. U.S.A. 84:8893-8897(1987) [PubMed: 3480517] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The amino acid sequence of delta 5-3-ketosteroid isomerase of Pseudomonas testosteroni."
Benson A.M., Jarabak R., Talalay P.
J. Biol. Chem. 246:7514-7525(1971) [PubMed: 5135313] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE.
[4]"Molecular weight determination and structural studies of Pseudomonas testosteroni delta 5 leads to 4-3-oxosteroid isomerase (EC 5.3.3.1)."
Weintraub H., Vincent F., Baulieu E.-E., Alfsen A.
FEBS Lett. 37:82-88(1973) [PubMed: 4753764] [Abstract]
Cited for: CHARACTERIZATION.
[5]"High-resolution crystal structures of delta5-3-ketosteroid isomerase with and without a reaction intermediate analogue."
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.
Biochemistry 36:14030-14036(1997) [PubMed: 9369474] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[6]"Solution structure of 3-oxo-delta5-steroid isomerase."
Wu Z.R., Ebrahimian S., Zawrotny M.E., Thornburg L.D., Perez-Alvarado G.C., Brothers P., Pollack R.M., Summers M.F.
Science 276:415-418(1997) [PubMed: 9103200] [Abstract]
Cited for: STRUCTURE BY NMR, MUTAGENESIS OF ASP-99.
[7]"Solution structure of delta 5-3-ketosteroid isomerase complexed with the steroid 19-nortestosterone hemisuccinate."
Massiah M.A., Abeygunawardana C., Gittis A.G., Mildvan A.S.
Biochemistry 37:14701-14712(1998) [PubMed: 9778345] [Abstract]
Cited for: STRUCTURE BY NMR IN COMPLEX WITH PRODUCT ANALOG.
[8]"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."
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.
J. Biol. Chem. 274:32863-32868(1999) [PubMed: 10551849] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH REACTION INTERMEDIATE ANALOG.
[9]"The conserved cis-Pro39 residue plays a crucial role in the proper positioning of the catalytic base Asp38 in ketosteroid isomerase from Comamonas testosteroni."
Nam G.H., Cha S.-S., Yun Y.S., Oh Y.H., Hong B.H., Lee H.-S., Choi K.-Y.
Biochem. J. 375:297-305(2003) [PubMed: 12852789] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT ALA-39 IN COMPLEX WITH REACTION INTERMEDIATE ANALOG.
[10]"Origin of the different pH activity profile in two homologous ketosteroid isomerases."
Yun Y.S., Lee T.-H., Nam G.H., Jang do S., Shin S., Oh B.-H., Choi K.-Y.
J. Biol. Chem. 278:28229-28236(2003) [PubMed: 12734184] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT TRP-116.
+Additional computationally mapped references.

Cross-references

Sequence databases

M22749 Genomic DNA. Translation: AAA25872.1.
J03568 Genomic DNA. Translation: AAA25871.1.
PIRSIPSDT. JT0336.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1BUQNMR-A/B1-125[»]
1ISKNMR-A/B1-125[»]
1OCVX-ray2.00A/B/C/D1-125[»]
1OGZX-ray2.30A1-125[»]
1OHPX-ray1.53A/B/C/D1-125[»]
1OHSX-ray1.70A/B/C/D1-125[»]
1QJGX-ray2.30A/B/C/D/E/F1-125[»]
8CHOX-ray2.30A1-125[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA5.3.3.1. 4566.

Family and domain databases

InterProIPR002075. NTF2.
IPR011944. Steroid_delta5-4_isomerase.
[Graphical view]
PfamPF02136. NTF2. 1 hit.
[Graphical view]
TIGRFAMsTIGR02246. CHP2246. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSDIS_COMTE
AccessionPrimary (citable) accession number: P00947
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1991
Last modified: June 16, 2009
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents