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KYNB_DEIGD
ID   KYNB_DEIGD              Reviewed;         213 AA.
AC   Q1IY56;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Kynurenine formamidase {ECO:0000255|HAMAP-Rule:MF_01969};
DE            Short=KFA {ECO:0000255|HAMAP-Rule:MF_01969};
DE            Short=KFase {ECO:0000255|HAMAP-Rule:MF_01969};
DE            EC=3.5.1.9 {ECO:0000255|HAMAP-Rule:MF_01969};
DE   AltName: Full=Arylformamidase {ECO:0000255|HAMAP-Rule:MF_01969};
DE   AltName: Full=N-formylkynurenine formamidase {ECO:0000255|HAMAP-Rule:MF_01969};
DE            Short=FKF {ECO:0000255|HAMAP-Rule:MF_01969};
GN   Name=kynB {ECO:0000255|HAMAP-Rule:MF_01969}; OrderedLocusNames=Dgeo_1533;
OS   Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=319795;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11300 / AG-3a;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA   Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-
CC       kynurenine, the second step in the kynurenine pathway of tryptophan
CC       degradation. {ECO:0000255|HAMAP-Rule:MF_01969}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-formyl-L-kynurenine = formate + H(+) + L-kynurenine;
CC         Xref=Rhea:RHEA:13009, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:57959, ChEBI:CHEBI:58629; EC=3.5.1.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01969};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01969};
CC       Note=Binds 2 zinc ions per subunit. {ECO:0000255|HAMAP-Rule:MF_01969};
CC   -!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via
CC       kynurenine pathway; L-kynurenine from L-tryptophan: step 2/2.
CC       {ECO:0000255|HAMAP-Rule:MF_01969}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01969}.
CC   -!- SIMILARITY: Belongs to the Cyclase 1 superfamily. KynB family.
CC       {ECO:0000255|HAMAP-Rule:MF_01969}.
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DR   EMBL; CP000359; ABF45828.1; -; Genomic_DNA.
DR   RefSeq; WP_011530662.1; NC_008025.1.
DR   AlphaFoldDB; Q1IY56; -.
DR   SMR; Q1IY56; -.
DR   STRING; 319795.Dgeo_1533; -.
DR   PRIDE; Q1IY56; -.
DR   EnsemblBacteria; ABF45828; ABF45828; Dgeo_1533.
DR   KEGG; dge:Dgeo_1533; -.
DR   eggNOG; COG1878; Bacteria.
DR   HOGENOM; CLU_030671_3_1_0; -.
DR   OMA; GHPTHKT; -.
DR   OrthoDB; 831439at2; -.
DR   UniPathway; UPA00333; UER00454.
DR   Proteomes; UP000002431; Chromosome.
DR   GO; GO:0004061; F:arylformamidase activity; ISS:UniProtKB.
DR   GO; GO:0004328; F:formamidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043420; P:anthranilate metabolic process; ISS:UniProtKB.
DR   GO; GO:0019441; P:tryptophan catabolic process to kynurenine; ISS:UniProtKB.
DR   Gene3D; 3.50.30.50; -; 1.
DR   HAMAP; MF_01969; KynB; 1.
DR   InterPro; IPR007325; KFase/CYL.
DR   InterPro; IPR037175; KFase_sf.
DR   InterPro; IPR017484; Kynurenine_formamidase_bac.
DR   PANTHER; PTHR31118; PTHR31118; 1.
DR   Pfam; PF04199; Cyclase; 1.
DR   SUPFAM; SSF102198; SSF102198; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome; Tryptophan catabolism; Zinc.
FT   CHAIN           1..213
FT                   /note="Kynurenine formamidase"
FT                   /id="PRO_0000362121"
FT   ACT_SITE        55
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT   BINDING         15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT   BINDING         45
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT   BINDING         49
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT   BINDING         51
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT   BINDING         51
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT   BINDING         157
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT   BINDING         169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT   BINDING         169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
SQ   SEQUENCE   213 AA;  22785 MW;  F06679FFA4C5838C CRC64;
     MIDISRQLTP SHPNWPGDAP FRVKPGARIA QGDSVNTGEL CTSTHTGTHV DAPWHYSETG
     ARLEEVELNR YVGRCRVVTV RAEGGLIPAA ALAGLPKRLP PRLLLHTGQP AHWTEFPEDF
     AALDPALIRE AARRGVRLIG TDSPSVDPLT SKTLDAHHAC LETDTLILEG LNLAEVPDGE
     YDLVCLPLPL AEVDGAPARA ILLPAGTLPE GEG
 
 
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