SDIS_PSEPU
ID SDIS_PSEPU Reviewed; 131 AA.
AC P07445;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Steroid Delta-isomerase;
DE EC=5.3.3.1;
DE AltName: Full=Delta(5)-3-ketosteroid isomerase;
GN Name=ksi;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Biotype B;
RX PubMed=7961420; DOI=10.1128/jb.176.21.6672-6676.1994;
RA Kim S.W., Kim C.Y., Benisek W.F., Choi K.Y.;
RT "Cloning, nucleotide sequence, and overexpression of the gene coding for
RT delta 5-3-ketosteroid isomerase from Pseudomonas putida biotype B.";
RL J. Bacteriol. 176:6672-6676(1994).
RN [2]
RP PROTEIN SEQUENCE.
RC STRAIN=Biotype B;
RX PubMed=3700400; DOI=10.1016/s0021-9258(19)84584-2;
RA Linden K.G., Benisek W.F.;
RT "The amino acid sequence of a delta 5-3-oxosteroid isomerase from
RT Pseudomonas putida biotype B.";
RL J. Biol. Chem. 261:6454-6460(1986).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH REACTION INTERMEDIATE
RP ANALOG, AND MUTAGENESIS OF TYR-16 AND ASP-103.
RX PubMed=9369474; DOI=10.1021/bi971546+;
RA Kim S.-W., Cha S.-S., Cho H.-S., Kim J.-S., Ha N.-C., Cho M.-J., Joo S.,
RA Kim K.-K., Choi K.-Y., Oh B.-H.;
RT "High-resolution crystal structures of delta5-3-ketosteroid isomerase with
RT and without a reaction intermediate analogue.";
RL Biochemistry 36:14030-14036(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=10529226; DOI=10.1021/bi991040m;
RA Kim D.-H., Nam G.H., Jang D.S., Choi G., Joo S., Kim J.-S., Oh B.-H.,
RA Choi K.-Y.;
RT "Roles of active site aromatic residues in catalysis by ketosteroid
RT isomerase from Pseudomonas putida biotype B.";
RL Biochemistry 38:13810-13819(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT ASN-40/GLU-103 IN COMPLEX
RP WITH REACTION INTERMEDIATE ANALOG, AND MUTAGENESIS OF TYR-16 AND ASP-103.
RX PubMed=10653633; DOI=10.1021/bi991579k;
RA Choi G., Ha N.-C., Kim S.W., Kim D.-H., Park S., Oh B.-H., Choi K.-Y.;
RT "Asp-99 donates a hydrogen bond not to Tyr-14 but to the steroid directly
RT in the catalytic mechanism of delta 5-3-ketosteroid isomerase from
RT Pseudomonas putida biotype B.";
RL Biochemistry 39:903-909(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
RX PubMed=11007792; DOI=10.1074/jbc.m007561200;
RA Ha N.-C., Kim M.-S., Lee W., Choi K.-Y., Oh B.-H.;
RT "Detection of large pKa perturbations of an inhibitor and a catalytic group
RT at an enzyme active site, a mechanistic basis for catalytic power of many
RT enzymes.";
RL J. Biol. Chem. 275:41100-41106(2000).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT SER-57, AND MUTAGENESIS OF
RP TYR-16 AND TYR-32.
RX PubMed=11695900; DOI=10.1021/bi015547k;
RA Nam G.H., Jang D.S., Cha S.-S., Lee T.-H., Kim D.-H., Hong B.H., Yun Y.S.,
RA Oh B.-H., Choi K.-Y.;
RT "Maintenance of alpha-helical structures by phenyl rings in the active-site
RT tyrosine triad contributes to catalysis and stability of ketosteroid
RT isomerase from Pseudomonas putida biotype B.";
RL Biochemistry 40:13529-13537(2001).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-92, AND MUTAGENESIS OF
RP LEU-125 AND VAL-127.
RX PubMed=15819891; DOI=10.1111/j.1742-4658.2005.04627.x;
RA Yun Y.S., Nam G.H., Kim Y.-G., Oh B.-H., Choi K.-Y.;
RT "Small exterior hydrophobic cluster contributes to conformational stability
RT and steroid binding in ketosteroid isomerase from Pseudomonas putida
RT biotype B.";
RL FEBS J. 272:1999-2011(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid;
CC Xref=Rhea:RHEA:14709, ChEBI:CHEBI:47907, ChEBI:CHEBI:47909;
CC EC=5.3.3.1;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10653633,
CC ECO:0000269|PubMed:11007792, ECO:0000269|PubMed:9369474}.
CC -!- INDUCTION: By steroids.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L13127; AAA64437.1; -; Genomic_DNA.
DR PIR; A25216; SIPSDP.
DR PDB; 1C7H; X-ray; 2.50 A; A=1-131.
DR PDB; 1CQS; X-ray; 1.90 A; A/B=1-131.
DR PDB; 1DMM; X-ray; 1.90 A; A=1-131.
DR PDB; 1DMN; X-ray; 2.05 A; A=1-131.
DR PDB; 1DMQ; X-ray; 2.15 A; A=1-131.
DR PDB; 1E3R; X-ray; 2.50 A; A/B=1-131.
DR PDB; 1E3V; X-ray; 2.00 A; A/B=1-131.
DR PDB; 1E97; X-ray; 2.00 A; A=1-131.
DR PDB; 1EA2; X-ray; 1.80 A; A=1-131.
DR PDB; 1GS3; X-ray; 2.10 A; A=1-131.
DR PDB; 1K41; X-ray; 2.20 A; A/B=1-131.
DR PDB; 1OGX; X-ray; 2.00 A; A/B=1-131.
DR PDB; 1OH0; X-ray; 1.10 A; A/B=1-131.
DR PDB; 1OHO; X-ray; 1.90 A; A=1-131.
DR PDB; 1OPY; X-ray; 1.90 A; A=1-131.
DR PDB; 1VZZ; X-ray; 2.30 A; A/B=1-131.
DR PDB; 1W00; X-ray; 2.20 A; A/B=1-131.
DR PDB; 1W01; X-ray; 2.20 A; A/B=1-131.
DR PDB; 1W02; X-ray; 2.30 A; A=1-131.
DR PDB; 1W6Y; X-ray; 2.10 A; A=1-131.
DR PDB; 2INX; X-ray; 1.50 A; A=1-131.
DR PDB; 2PZV; X-ray; 1.25 A; A/B/C/D=1-131.
DR PDB; 3CPO; X-ray; 1.24 A; A=1-131.
DR PDB; 3FZW; X-ray; 1.32 A; A/B=1-131.
DR PDB; 3IPT; X-ray; 1.63 A; A/B/C/D=1-131.
DR PDB; 3OWS; X-ray; 1.71 A; A/B/C/D=1-131.
DR PDB; 3OWU; X-ray; 1.70 A; A/B/C/D=1-131.
DR PDB; 3OWY; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-131.
DR PDB; 3OX9; X-ray; 2.00 A; A/B/C/D=1-131.
DR PDB; 3OXA; X-ray; 1.89 A; A/B/C/D=1-131.
DR PDB; 3RGR; X-ray; 1.59 A; A=1-131.
DR PDB; 3SED; X-ray; 1.30 A; A=3-127.
DR PDB; 3T8N; X-ray; 1.47 A; A/B/D/F=1-131.
DR PDB; 3VGN; X-ray; 1.30 A; A/B=1-131.
DR PDB; 3VSY; X-ray; 1.50 A; A/B=3-131.
DR PDB; 4CDL; X-ray; 2.50 A; A=1-131.
DR PDB; 4K1U; X-ray; 2.00 A; A/B=1-131.
DR PDB; 4K1V; X-ray; 1.80 A; A=1-131.
DR PDB; 5AI1; X-ray; 2.10 A; A=1-131.
DR PDB; 5D81; X-ray; 1.39 A; A=1-131.
DR PDB; 5D82; X-ray; 1.37 A; A/B=1-131.
DR PDB; 5D83; X-ray; 1.70 A; A/B=1-131.
DR PDB; 5G2G; X-ray; 1.60 A; A/B=2-128.
DR PDB; 5KP1; X-ray; 1.22 A; A/B/C/D=1-131.
DR PDB; 5KP3; X-ray; 1.70 A; A/B=1-131.
DR PDB; 5KP4; X-ray; 1.71 A; A/B=1-131.
DR PDB; 6C17; X-ray; 1.10 A; A=1-131.
DR PDB; 6C1J; X-ray; 1.06 A; A=1-131.
DR PDB; 6C1X; X-ray; 1.05 A; A=1-131.
DR PDB; 6F4Y; X-ray; 1.92 A; A/B=3-127.
DR PDB; 6F50; X-ray; 2.00 A; A/B=3-127.
DR PDB; 6F53; X-ray; 1.49 A; A=3-127.
DR PDB; 6F54; X-ray; 1.08 A; A/B=3-127.
DR PDB; 6TZD; X-ray; 1.45 A; A/B=1-131.
DR PDB; 6U1Z; X-ray; 1.50 A; A/B=1-131.
DR PDB; 6U4I; X-ray; 1.55 A; A/B=1-131.
DR PDB; 6UBQ; X-ray; 1.30 A; A/B=1-131.
DR PDB; 6UCN; X-ray; 1.32 A; A/B=1-131.
DR PDB; 6UCW; X-ray; 1.25 A; A/B=1-131.
DR PDB; 6UCY; X-ray; 1.15 A; A/B=1-131.
DR PDB; 6UFS; X-ray; 1.47 A; A/B=1-131.
DR PDBsum; 1C7H; -.
DR PDBsum; 1CQS; -.
DR PDBsum; 1DMM; -.
DR PDBsum; 1DMN; -.
DR PDBsum; 1DMQ; -.
DR PDBsum; 1E3R; -.
DR PDBsum; 1E3V; -.
DR PDBsum; 1E97; -.
DR PDBsum; 1EA2; -.
DR PDBsum; 1GS3; -.
DR PDBsum; 1K41; -.
DR PDBsum; 1OGX; -.
DR PDBsum; 1OH0; -.
DR PDBsum; 1OHO; -.
DR PDBsum; 1OPY; -.
DR PDBsum; 1VZZ; -.
DR PDBsum; 1W00; -.
DR PDBsum; 1W01; -.
DR PDBsum; 1W02; -.
DR PDBsum; 1W6Y; -.
DR PDBsum; 2INX; -.
DR PDBsum; 2PZV; -.
DR PDBsum; 3CPO; -.
DR PDBsum; 3FZW; -.
DR PDBsum; 3IPT; -.
DR PDBsum; 3OWS; -.
DR PDBsum; 3OWU; -.
DR PDBsum; 3OWY; -.
DR PDBsum; 3OX9; -.
DR PDBsum; 3OXA; -.
DR PDBsum; 3RGR; -.
DR PDBsum; 3SED; -.
DR PDBsum; 3T8N; -.
DR PDBsum; 3VGN; -.
DR PDBsum; 3VSY; -.
DR PDBsum; 4CDL; -.
DR PDBsum; 4K1U; -.
DR PDBsum; 4K1V; -.
DR PDBsum; 5AI1; -.
DR PDBsum; 5D81; -.
DR PDBsum; 5D82; -.
DR PDBsum; 5D83; -.
DR PDBsum; 5G2G; -.
DR PDBsum; 5KP1; -.
DR PDBsum; 5KP3; -.
DR PDBsum; 5KP4; -.
DR PDBsum; 6C17; -.
DR PDBsum; 6C1J; -.
DR PDBsum; 6C1X; -.
DR PDBsum; 6F4Y; -.
DR PDBsum; 6F50; -.
DR PDBsum; 6F53; -.
DR PDBsum; 6F54; -.
DR PDBsum; 6TZD; -.
DR PDBsum; 6U1Z; -.
DR PDBsum; 6U4I; -.
DR PDBsum; 6UBQ; -.
DR PDBsum; 6UCN; -.
DR PDBsum; 6UCW; -.
DR PDBsum; 6UCY; -.
DR PDBsum; 6UFS; -.
DR AlphaFoldDB; P07445; -.
DR SMR; P07445; -.
DR BindingDB; P07445; -.
DR ChEMBL; CHEMBL2321641; -.
DR DrugBank; DB03619; Deoxycholic acid.
DR DrugBank; DB03515; Equilenin.
DR DrugCentral; P07445; -.
DR BRENDA; 5.3.3.1; 5092.
DR EvolutionaryTrace; P07445; -.
DR GO; GO:0004769; F:steroid delta-isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00781; ketosteroid_isomerase; 1.
DR InterPro; IPR039256; Ketosteroid_isomerase.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR037401; SnoaL-like.
DR Pfam; PF12680; SnoaL_2; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Isomerase; Lipid metabolism;
KW Steroid metabolism.
FT CHAIN 1..131
FT /note="Steroid Delta-isomerase"
FT /id="PRO_0000097646"
FT ACT_SITE 16
FT /note="Proton donor"
FT ACT_SITE 40
FT /note="Proton acceptor"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11007792"
FT MUTAGEN 16
FT /note="Y->F: Reduces activity 2000-fold. Reduces activity
FT 10000-fold; when associated with E-103; N-103 or L-103."
FT /evidence="ECO:0000269|PubMed:10653633,
FT ECO:0000269|PubMed:11695900, ECO:0000269|PubMed:9369474"
FT MUTAGEN 16
FT /note="Y->S: Reduces activity 20-fold."
FT /evidence="ECO:0000269|PubMed:10653633,
FT ECO:0000269|PubMed:11695900, ECO:0000269|PubMed:9369474"
FT MUTAGEN 32
FT /note="Y->S: Reduces activity 4-fold."
FT /evidence="ECO:0000269|PubMed:11695900"
FT MUTAGEN 57
FT /note="Y->S: Reduces activity 100-fold."
FT MUTAGEN 92
FT /note="W->A: Slightly reduces activity. Reduces protein
FT stability."
FT MUTAGEN 103
FT /note="D->A,L: Reduces activity 100-fold. Reduces activity
FT 10000-fold; when associated with F-16."
FT /evidence="ECO:0000269|PubMed:10653633,
FT ECO:0000269|PubMed:9369474"
FT MUTAGEN 103
FT /note="D->E: Slightly reduces activity. Reduces activity
FT 10000-fold; when associated with F-16."
FT /evidence="ECO:0000269|PubMed:10653633,
FT ECO:0000269|PubMed:9369474"
FT MUTAGEN 103
FT /note="D->N: Reduces activity 4-fold. Reduces activity
FT 10000-fold; when associated with F-16."
FT /evidence="ECO:0000269|PubMed:10653633,
FT ECO:0000269|PubMed:9369474"
FT MUTAGEN 125
FT /note="L->A: Slightly reduces activity and reduces protein
FT stability; when associated with A-127."
FT /evidence="ECO:0000269|PubMed:15819891"
FT MUTAGEN 127
FT /note="V->A: Slightly reduces activity and reduces protein
FT stability; when associated with A-125."
FT /evidence="ECO:0000269|PubMed:15819891"
FT HELIX 6..22
FT /evidence="ECO:0007829|PDB:6C1X"
FT HELIX 25..30
FT /evidence="ECO:0007829|PDB:6C1X"
FT STRAND 32..41
FT /evidence="ECO:0007829|PDB:6C1X"
FT HELIX 49..61
FT /evidence="ECO:0007829|PDB:6C1X"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:6C1J"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:6C1X"
FT STRAND 78..92
FT /evidence="ECO:0007829|PDB:6C1X"
FT STRAND 95..107
FT /evidence="ECO:0007829|PDB:6C1X"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:6C1X"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:6C1X"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:6UCY"
SQ SEQUENCE 131 AA; 14536 MW; 08711198C13CF014 CRC64;
MNLPTAQEVQ GLMARYIELV DVGDIEAIVQ MYADDATVED PFGQPPIHGR EQIAAFYRQG
LGGGKVRACL TGPVRASHNG CGAMPFRVEM VWNGQPCALD VIDVMRFDEH GRIQTMQAYW
SEVNLSVREP Q
