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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)DescriptionActionsGraphical viewLength
Active sitei16Proton donor1
Active sitei40Proton acceptor1
Binding sitei103Substrate1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomerase
Biological processLipid 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)DescriptionActionsGraphical viewLength
Mutagenesisi16Y → F: Reduces activity 2000-fold. Reduces activity 10000-fold; when associated with E-103; N-103 or L-103. 3 Publications1
Mutagenesisi16Y → S: Reduces activity 20-fold. 3 Publications1
Mutagenesisi32Y → S: Reduces activity 4-fold. 1 Publication1
Mutagenesisi57Y → S: Reduces activity 100-fold. 1
Mutagenesisi92W → A: Slightly reduces activity. Reduces protein stability. 1
Mutagenesisi103D → A or L: Reduces activity 100-fold. Reduces activity 10000-fold; when associated with F-16. 2 Publications1
Mutagenesisi103D → E: Slightly reduces activity. Reduces activity 10000-fold; when associated with F-16. 2 Publications1
Mutagenesisi103D → N: Reduces activity 4-fold. Reduces activity 10000-fold; when associated with F-16. 2 Publications1
Mutagenesisi125L → A: Slightly reduces activity and reduces protein stability; when associated with A-127. 1 Publication1
Mutagenesisi127V → A: Slightly reduces activity and reduces protein stability; when associated with A-125. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL2321641.
DrugBankiDB03619. Deoxycholic Acid.
DB03515. Equilenin.
DB01708. Prasterone.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000976461 – 131Steroid Delta-isomeraseAdd BLAST131

Expressioni

Inductioni

By steroids.

Interactioni

Subunit structurei

Homodimer.3 Publications

Chemistry databases

BindingDBiP07445.

Structurei

Secondary structure

1131
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 22Combined sources17
Helixi25 – 31Combined sources7
Beta strandi32 – 41Combined sources10
Helixi49 – 61Combined sources13
Beta strandi62 – 64Combined sources3
Beta strandi67 – 72Combined sources6
Beta strandi78 – 107Combined sources30
Beta strandi113 – 119Combined sources7
Helixi122 – 124Combined sources3
Beta strandi125 – 127Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5G2GX-ray1.60A/B2-128[»]
5KP1X-ray1.22A/B/C/D1-131[»]
5KP3X-ray1.70A/B1-131[»]
5KP4X-ray1.71A/B1-131[»]
ProteinModelPortaliP07445.
SMRiP07445.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07445.

Family & Domainsi

Family and domain databases

Gene3Di3.10.450.50. 1 hit.
InterProiView protein in InterPro
IPR009959. Cyclase_SnoaL-like_dom.
IPR032710. NTF2-like_dom.
PfamiView protein in Pfam
PF12680. SnoaL_2. 1 hit.
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
PDB 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[»]
5G2GX-ray1.60A/B2-128[»]
5KP1X-ray1.22A/B/C/D1-131[»]
5KP3X-ray1.70A/B1-131[»]
5KP4X-ray1.71A/B1-131[»]
ProteinModelPortaliP07445.
SMRiP07445.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP07445.
ChEMBLiCHEMBL2321641.
DrugBankiDB03619. Deoxycholic Acid.
DB03515. Equilenin.
DB01708. Prasterone.

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.
InterProiView protein in InterPro
IPR009959. Cyclase_SnoaL-like_dom.
IPR032710. NTF2-like_dom.
PfamiView protein in Pfam
PF12680. SnoaL_2. 1 hit.
SUPFAMiSSF54427. SSF54427. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSDIS_PSEPU
AccessioniPrimary (citable) accession number: P07445
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: March 15, 2017
This is version 99 of the entry and version 1 of the sequence. See 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.