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Protein

Steroid Delta-isomerase

Gene

ksi

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: 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

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. 5092.

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

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

Chemistry

ChEMBLiCHEMBL2321641.

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

Chemistry

BindingDBiP07445.

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[»]
4CDLX-ray2.50A1-131[»]
4K1UX-ray2.00A/B1-131[»]
4K1VX-ray1.80A1-131[»]
5AI1X-ray2.10A1-131[»]
5D81X-ray1.39A1-131[»]
5D82X-ray1.37A/B1-131[»]
5D83X-ray1.70A/B1-131[»]
ProteinModelPortaliP07445.
SMRiP07445. Positions 2-130.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07445.

Family & Domainsi

Family and domain databases

Gene3Di3.10.450.50. 1 hit.
InterProiIPR009959. Cyclase_SnoaL-like_dom.
IPR032710. NTF2-like_dom.
[Graphical view]
PfamiPF12680. SnoaL_2. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.

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.
PIRiA25216. SIPSDP.

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[»]
4CDLX-ray2.50A1-131[»]
4K1UX-ray2.00A/B1-131[»]
4K1VX-ray1.80A1-131[»]
5AI1X-ray2.10A1-131[»]
5D81X-ray1.39A1-131[»]
5D82X-ray1.37A/B1-131[»]
5D83X-ray1.70A/B1-131[»]
ProteinModelPortaliP07445.
SMRiP07445. Positions 2-130.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP07445.
ChEMBLiCHEMBL2321641.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi5.3.3.1. 5092.

Miscellaneous databases

EvolutionaryTraceiP07445.

Family and domain databases

Gene3Di3.10.450.50. 1 hit.
InterProiIPR009959. Cyclase_SnoaL-like_dom.
IPR032710. NTF2-like_dom.
[Graphical view]
PfamiPF12680. SnoaL_2. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.
ProtoNetiSearch...

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: February 17, 2016
This is version 96 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

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.