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Protein

Steroid Delta-isomerase

Gene

ksi

Organism
Comamonas testosteroni (Pseudomonas testosteroni)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei14 – 141Proton donor
Active sitei38 – 381Proton acceptor1 Publication
Binding sitei99 – 991Substrate

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Lipid metabolism, Steroid metabolism

Enzyme and pathway databases

BRENDAi5.3.3.1. 1590.
SABIO-RKP00947.

Names & Taxonomyi

Protein namesi
Recommended name:
Steroid Delta-isomerase (EC:5.3.3.1)
Alternative name(s):
Delta(5)-3-ketosteroid isomerase
Gene namesi
Name:ksi
OrganismiComamonas testosteroni (Pseudomonas testosteroni)
Taxonomic identifieri285 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeComamonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi39 – 391P → A: Perturbs active site geometry and lowers activity.
Mutagenesisi99 – 991D → A: Lowers activity 3000-fold. 1 Publication
Mutagenesisi116 – 1161F → W: Slightly lower activity at neutral pH. Increased catalytic activity at pH 3.8.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 125125Steroid Delta-isomerasePRO_0000097644Add
BLAST

Expressioni

Inductioni

By steroids.

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

STRINGi688245.CtCNB1_1323.

Structurei

Secondary structure

1
125
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2017Combined sources
Helixi23 – 275Combined sources
Beta strandi30 – 3910Combined sources
Beta strandi45 – 473Combined sources
Helixi48 – 5811Combined sources
Beta strandi64 – 674Combined sources
Beta strandi72 – 743Combined sources
Beta strandi77 – 8812Combined sources
Beta strandi91 – 955Combined sources
Beta strandi98 – 1036Combined sources
Turni105 – 1073Combined sources
Beta strandi109 – 1157Combined sources
Helixi118 – 1203Combined sources
Beta strandi121 – 1233Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
3M8CX-ray2.10A/B/C/D1-125[»]
3MHEX-ray1.72A/B1-125[»]
3MKIX-ray2.00A/B/C/D1-125[»]
3MYTX-ray1.96A/B/C/D1-125[»]
3NBRX-ray1.73A1-125[»]
3NHXX-ray1.59A1-125[»]
3NM2X-ray1.89A1-125[»]
3NUVX-ray1.76A/B1-125[»]
3NXJX-ray1.97A/B1-125[»]
3OV4X-ray1.83A/B/C/D1-125[»]
3T8UX-ray2.50A/B/C/D1-125[»]
3UNLX-ray2.52A/B/C/D1-125[»]
4L7KX-ray2.10A/B/C/D/E/F/G/H/I/J/K/O1-125[»]
8CHOX-ray2.30A1-125[»]
ProteinModelPortaliP00947.
SMRiP00947. Positions 1-125.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00947.

Family & Domainsi

Phylogenomic databases

eggNOGiENOG4105X1P. Bacteria.
ENOG411288K. LUCA.

Family and domain databases

Gene3Di3.10.450.50. 1 hit.
InterProiIPR002075. NTF2.
IPR032710. NTF2-like_dom.
IPR011944. Steroid_delta5-4_isomerase.
[Graphical view]
PfamiPF02136. NTF2. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.
TIGRFAMsiTIGR02246. TIGR02246. 1 hit.

Sequencei

Sequence statusi: Complete.

P00947-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTPEHMTAV VQRYVAALNA GDLDGIVALF ADDATVEDPV GSEPRSGTAA
60 70 80 90 100
IREFYANSLK LPLAVELTQE VRAVANEAAF AFTVSFEYQG RKTVVAPIDH
110 120
FRFNGAGKVV SMRALFGEKN IHAGA
Length:125
Mass (Da):13,398
Last modified:February 1, 1991 - v2
Checksum:i2ECD410D4B929430
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22749 Genomic DNA. Translation: AAA25872.1.
J03568 Genomic DNA. Translation: AAA25871.1.
PIRiJT0336. SIPSDT.
RefSeqiWP_003078309.1. NZ_BBJZ01000017.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22749 Genomic DNA. Translation: AAA25872.1.
J03568 Genomic DNA. Translation: AAA25871.1.
PIRiJT0336. SIPSDT.
RefSeqiWP_003078309.1. NZ_BBJZ01000017.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
3M8CX-ray2.10A/B/C/D1-125[»]
3MHEX-ray1.72A/B1-125[»]
3MKIX-ray2.00A/B/C/D1-125[»]
3MYTX-ray1.96A/B/C/D1-125[»]
3NBRX-ray1.73A1-125[»]
3NHXX-ray1.59A1-125[»]
3NM2X-ray1.89A1-125[»]
3NUVX-ray1.76A/B1-125[»]
3NXJX-ray1.97A/B1-125[»]
3OV4X-ray1.83A/B/C/D1-125[»]
3T8UX-ray2.50A/B/C/D1-125[»]
3UNLX-ray2.52A/B/C/D1-125[»]
4L7KX-ray2.10A/B/C/D/E/F/G/H/I/J/K/O1-125[»]
8CHOX-ray2.30A1-125[»]
ProteinModelPortaliP00947.
SMRiP00947. Positions 1-125.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi688245.CtCNB1_1323.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105X1P. Bacteria.
ENOG411288K. LUCA.

Enzyme and pathway databases

BRENDAi5.3.3.1. 1590.
SABIO-RKP00947.

Miscellaneous databases

EvolutionaryTraceiP00947.

Family and domain databases

Gene3Di3.10.450.50. 1 hit.
InterProiIPR002075. NTF2.
IPR032710. NTF2-like_dom.
IPR011944. Steroid_delta5-4_isomerase.
[Graphical view]
PfamiPF02136. NTF2. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.
TIGRFAMsiTIGR02246. TIGR02246. 1 hit.
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  6. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT TRP-116.

Entry informationi

Entry nameiSDIS_COMTE
AccessioniPrimary (citable) accession number: P00947
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1991
Last modified: June 8, 2016
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.