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P07445

- SDIS_PSEPU

UniProt

P07445 - SDIS_PSEPU

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Protein

Steroid Delta-isomerase

Gene

ksi

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed - Annotation score: 5 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 sitei16 – 161Proton donor
Active sitei40 – 401Proton acceptor
Binding sitei103 – 1031Substrate1 Publication

GO - Molecular functioni

  1. steroid delta-isomerase activity Source: UniProtKB-EC

GO - Biological processi

  1. steroid metabolic process Source: UniProtKB-KW
  2. transport Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Lipid metabolism, Steroid metabolism

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
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Subcellular locationi

GO - Cellular componenti

  1. intracellular Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi16 – 161Y → F: Reduces activity 2000-fold. Reduces activity 10000-fold; when associated with E-103; N-103 or L-103. 3 Publications
Mutagenesisi16 – 161Y → S: Reduces activity 20-fold. 3 Publications
Mutagenesisi32 – 321Y → S: Reduces activity 4-fold. 1 Publication
Mutagenesisi57 – 571Y → S: Reduces activity 100-fold.
Mutagenesisi92 – 921W → A: Slightly reduces activity. Reduces protein stability.
Mutagenesisi103 – 1031D → A or L: Reduces activity 100-fold. Reduces activity 10000-fold; when associated with F-16. 2 Publications
Mutagenesisi103 – 1031D → E: Slightly reduces activity. Reduces activity 10000-fold; when associated with F-16. 2 Publications
Mutagenesisi103 – 1031D → N: Reduces activity 4-fold. Reduces activity 10000-fold; when associated with F-16. 2 Publications
Mutagenesisi125 – 1251L → A: Slightly reduces activity and reduces protein stability; when associated with A-127. 1 Publication
Mutagenesisi127 – 1271V → A: Slightly reduces activity and reduces protein stability; when associated with A-125. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 131131Steroid Delta-isomerasePRO_0000097646Add
BLAST

Expressioni

Inductioni

By steroids.

Interactioni

Subunit structurei

Homodimer.3 Publications

Structurei

Secondary structure

1
131
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 2217Combined sources
Helixi25 – 317Combined sources
Beta strandi32 – 4110Combined sources
Helixi49 – 6113Combined sources
Beta strandi62 – 643Combined sources
Beta strandi67 – 726Combined sources
Beta strandi78 – 10730Combined sources
Beta strandi113 – 1197Combined sources
Helixi122 – 1243Combined sources
Beta strandi125 – 1273Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP07445.
SMRiP07445. Positions 2-130.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07445.

Family & Domainsi

Family and domain databases

InterProiIPR009959. Cyclase_SnoaL-like_dom.
IPR002075. NTF2.
[Graphical view]
PfamiPF02136. NTF2. 1 hit.
PF12680. SnoaL_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07445-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNLPTAQEVQ GLMARYIELV DVGDIEAIVQ MYADDATVED PFGQPPIHGR
60 70 80 90 100
EQIAAFYRQG LGGGKVRACL TGPVRASHNG CGAMPFRVEM VWNGQPCALD
110 120 130
VIDVMRFDEH GRIQTMQAYW SEVNLSVREP Q
Length:131
Mass (Da):14,536
Last modified:April 1, 1988 - v1
Checksum:i08711198C13CF014
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13127 Genomic DNA. Translation: AAA64437.1.
PIRiA25216. SIPSDP.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13127 Genomic DNA. Translation: AAA64437.1 .
PIRi A25216. SIPSDP.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C7H X-ray 2.50 A 1-131 [» ]
1CQS X-ray 1.90 A/B 1-131 [» ]
1DMM X-ray 1.90 A 1-131 [» ]
1DMN X-ray 2.05 A 1-131 [» ]
1DMQ X-ray 2.15 A 1-131 [» ]
1E3R X-ray 2.50 A/B 1-131 [» ]
1E3V X-ray 2.00 A/B 1-131 [» ]
1E97 X-ray 2.00 A 1-131 [» ]
1EA2 X-ray 1.80 A 1-131 [» ]
1GS3 X-ray 2.10 A 1-131 [» ]
1K41 X-ray 2.20 A/B 1-131 [» ]
1OGX X-ray 2.00 A/B 1-131 [» ]
1OH0 X-ray 1.10 A/B 1-131 [» ]
1OHO X-ray 1.90 A 1-131 [» ]
1OPY X-ray 1.90 A 1-131 [» ]
1VZZ X-ray 2.30 A/B 1-131 [» ]
1W00 X-ray 2.20 A/B 1-131 [» ]
1W01 X-ray 2.20 A/B 1-131 [» ]
1W02 X-ray 2.30 A 1-131 [» ]
1W6Y X-ray 2.10 A 1-131 [» ]
2INX X-ray 1.50 A 1-131 [» ]
2PZV X-ray 1.25 A/B/C/D 1-131 [» ]
3CPO X-ray 1.24 A 1-131 [» ]
3FZW X-ray 1.32 A/B 1-131 [» ]
3IPT X-ray 1.63 A/B/C/D 1-131 [» ]
3OWS X-ray 1.71 A/B/C/D 1-131 [» ]
3OWU X-ray 1.70 A/B/C/D 1-131 [» ]
3OWY X-ray 2.30 A/B/C/D/E/F/G/H 1-131 [» ]
3OX9 X-ray 2.00 A/B/C/D 1-131 [» ]
3OXA X-ray 1.89 A/B/C/D 1-131 [» ]
3RGR X-ray 1.59 A 1-131 [» ]
3SED X-ray 1.30 A 3-127 [» ]
3T8N X-ray 1.47 A/B/D/F 1-131 [» ]
3VGN X-ray 1.30 A/B 1-131 [» ]
3VSY X-ray 1.50 A/B 3-131 [» ]
4K1U X-ray 2.00 A/B 1-131 [» ]
4K1V X-ray 1.80 A 1-131 [» ]
ProteinModelPortali P07445.
SMRi P07445. Positions 2-130.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P07445.
ChEMBLi CHEMBL2321641.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P07445.

Family and domain databases

InterProi IPR009959. Cyclase_SnoaL-like_dom.
IPR002075. NTF2.
[Graphical view ]
Pfami PF02136. NTF2. 1 hit.
PF12680. SnoaL_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiSDIS_PSEPU
AccessioniPrimary (citable) accession number: P07445
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: November 26, 2014
This is version 89 of the entry and version 1 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

External Data

Dasty 3