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P07445 (SDIS_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length131 AA.
Sequence statusComplete.
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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 131131Steroid Delta-isomerase
PRO_0000097646

Sites

Active site161Proton donor
Active site401Proton acceptor
Binding site1031Substrate

Experimental info

Mutagenesis161Y → F: Reduces activity 2000-fold. Reduces activity 10000-fold; when associated with E-103; N-103 or L-103. Ref.3 Ref.5 Ref.7
Mutagenesis161Y → S: Reduces activity 20-fold. Ref.3 Ref.5 Ref.7
Mutagenesis321Y → S: Reduces activity 4-fold. Ref.7
Mutagenesis571Y → S: Reduces activity 100-fold.
Mutagenesis921W → A: Slightly reduces activity. Reduces protein stability.
Mutagenesis1031D → A or L: Reduces activity 100-fold. Reduces activity 10000-fold; when associated with F-16. Ref.3 Ref.5
Mutagenesis1031D → E: Slightly reduces activity. Reduces activity 10000-fold; when associated with F-16. Ref.3 Ref.5
Mutagenesis1031D → N: Reduces activity 4-fold. Reduces activity 10000-fold; when associated with F-16. Ref.3 Ref.5
Mutagenesis1251L → A: Slightly reduces activity and reduces protein stability; when associated with A-127. Ref.8
Mutagenesis1271V → A: Slightly reduces activity and reduces protein stability; when associated with A-125. Ref.8

Secondary structure

.................. 131
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07445 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 08711198C13CF014

FASTA13114,536
        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 

« Hide

References

[1]"Cloning, nucleotide sequence, and overexpression of the gene coding for delta 5-3-ketosteroid isomerase from Pseudomonas putida biotype B."
Kim S.W., Kim C.Y., Benisek W.F., Choi K.Y.
J. Bacteriol. 176:6672-6676(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Biotype B.
[2]"The amino acid sequence of a delta 5-3-oxosteroid isomerase from Pseudomonas putida biotype B."
Linden K.G., Benisek W.F.
J. Biol. Chem. 261:6454-6460(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: Biotype B.
[3]"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 (2.5 ANGSTROMS) IN COMPLEX WITH REACTION INTERMEDIATE ANALOG, MUTAGENESIS OF TYR-16 AND ASP-103.
[4]"Roles of active site aromatic residues in catalysis by ketosteroid isomerase from Pseudomonas putida biotype B."
Kim D.-H., Nam G.H., Jang D.S., Choi G., Joo S., Kim J.-S., Oh B.-H., Choi K.-Y.
Biochemistry 38:13810-13819(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[5]"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."
Choi G., Ha N.-C., Kim S.W., Kim D.-H., Park S., Oh B.-H., Choi K.-Y.
Biochemistry 39:903-909(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT ASN-40/GLU-103 IN COMPLEX WITH REACTION INTERMEDIATE ANALOG, MUTAGENESIS OF TYR-16 AND ASP-103.
[6]"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."
Ha N.-C., Kim M.-S., Lee W., Choi K.-Y., Oh B.-H.
J. Biol. Chem. 275:41100-41106(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
[7]"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."
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.
Biochemistry 40:13529-13537(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT SER-57, MUTAGENESIS OF TYR-16 AND TYR-32.
[8]"Small exterior hydrophobic cluster contributes to conformational stability and steroid binding in ketosteroid isomerase from Pseudomonas putida biotype B."
Yun Y.S., Nam G.H., Kim Y.-G., Oh B.-H., Choi K.-Y.
FEBS J. 272:1999-2011(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-92, MUTAGENESIS OF LEU-125 AND VAL-127.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L13127 Genomic DNA. Translation: AAA64437.1.
PIRSIPSDP. A25216.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C7HX-ray2.50A1-131[»]
1CQSX-ray1.90A/B1-131[»]
1DMMX-ray1.90A1-131[»]
1DMNX-ray2.05A1-131[»]
1DMQX-ray2.15A1-131[»]
1E3RX-ray2.50A/B1-131[»]
1E3VX-ray2.00A/B1-131[»]
1E97X-ray2.00A1-131[»]
1EA2X-ray1.80A1-131[»]
1GS3X-ray2.10A1-131[»]
1K41X-ray2.20A/B1-131[»]
1OGXX-ray2.00A/B1-131[»]
1OH0X-ray1.10A/B1-131[»]
1OHOX-ray1.90A1-131[»]
1OPYX-ray1.90A1-131[»]
1VZZX-ray2.30A/B1-131[»]
1W00X-ray2.20A/B1-131[»]
1W01X-ray2.20A/B1-131[»]
1W02X-ray2.30A1-131[»]
1W6YX-ray2.10A1-131[»]
2INXX-ray1.50A1-131[»]
2PZVX-ray1.25A/B/C/D1-131[»]
3CPOX-ray1.24A1-131[»]
3FZWX-ray1.32A/B1-131[»]
3IPTX-ray1.63A/B/C/D1-131[»]
3OWSX-ray1.71A/B/C/D1-131[»]
3OWUX-ray1.70A/B/C/D1-131[»]
3OWYX-ray2.30A/B/C/D/E/F/G/H1-131[»]
3OX9X-ray2.00A/B/C/D1-131[»]
3OXAX-ray1.89A/B/C/D1-131[»]
3RGRX-ray1.59A1-131[»]
3SEDX-ray1.30A3-127[»]
3T8NX-ray1.47A/B/D/F1-131[»]
3VGNX-ray1.30A/B1-131[»]
3VSYX-ray1.50A/B3-131[»]
4K1UX-ray2.00A/B1-131[»]
4K1VX-ray1.80A1-131[»]
ProteinModelPortalP07445.
SMRP07445. Positions 2-130.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL2321641.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR009959. Cyclase_SnoaL-like_dom.
IPR002075. NTF2.
[Graphical view]
PfamPF02136. NTF2. 1 hit.
PF12680. SnoaL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07445.

Entry information

Entry nameSDIS_PSEPU
AccessionPrimary (citable) accession number: P07445
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: November 13, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references