Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P07445

- SDIS_PSEPU

UniProt

P07445 - SDIS_PSEPU

Protein

Steroid Delta-isomerase

Gene

ksi

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    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

    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 – 2217
    Helixi25 – 317
    Beta strandi32 – 4110
    Helixi49 – 6113
    Beta strandi62 – 643
    Beta strandi67 – 726
    Beta strandi78 – 10730
    Beta strandi113 – 1197
    Helixi122 – 1243
    Beta strandi125 – 1273

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MNLPTAQEVQ GLMARYIELV DVGDIEAIVQ MYADDATVED PFGQPPIHGR    50
    EQIAAFYRQG LGGGKVRACL TGPVRASHNG CGAMPFRVEM VWNGQPCALD 100
    VIDVMRFDEH GRIQTMQAYW SEVNLSVREP Q 131
    Length:131
    Mass (Da):14,536
    Last modified:April 1, 1988 - v1
    Checksum:i08711198C13CF014
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L13127 Genomic DNA. Translation: AAA64437.1.
    PIRiA25216. SIPSDP.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L13127 Genomic DNA. Translation: AAA64437.1 .
    PIRi A25216. SIPSDP.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    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: October 1, 2014
    This is version 88 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