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KFA_CANAL
ID   KFA_CANAL               Reviewed;         267 AA.
AC   Q59ZV4; A0A1D8PFW7;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Kynurenine formamidase {ECO:0000255|HAMAP-Rule:MF_03014};
DE            Short=KFA {ECO:0000255|HAMAP-Rule:MF_03014};
DE            Short=KFase {ECO:0000255|HAMAP-Rule:MF_03014};
DE            EC=3.5.1.9 {ECO:0000255|HAMAP-Rule:MF_03014};
DE   AltName: Full=Arylformamidase {ECO:0000255|HAMAP-Rule:MF_03014};
DE   AltName: Full=N-formylkynurenine formamidase {ECO:0000255|HAMAP-Rule:MF_03014};
DE            Short=FKF {ECO:0000255|HAMAP-Rule:MF_03014};
GN   Name=BNA7 {ECO:0000255|HAMAP-Rule:MF_03014};
GN   OrderedLocusNames=CAALFM_C114270WA; ORFNames=CaO19.7237;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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. Kynurenine may be further oxidized to nicotinic acid,
CC       NAD(H) and NADP(H). Required for elimination of toxic metabolites.
CC       {ECO:0000255|HAMAP-Rule:MF_03014}.
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_03014};
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_03014}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03014}.
CC   -!- DOMAIN: The main chain amide nitrogen atoms of the second glycine and
CC       its adjacent residue in the HGGXW motif define the oxyanion hole, and
CC       stabilize the oxyanion that forms during the nucleophilic attack by the
CC       catalytic serine during substrate cleavage. {ECO:0000255|HAMAP-
CC       Rule:MF_03014}.
CC   -!- SIMILARITY: Belongs to the kynurenine formamidase family.
CC       {ECO:0000255|HAMAP-Rule:MF_03014}.
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DR   EMBL; CP017623; AOW27027.1; -; Genomic_DNA.
DR   RefSeq; XP_715037.1; XM_709944.1.
DR   AlphaFoldDB; Q59ZV4; -.
DR   SMR; Q59ZV4; -.
DR   STRING; 237561.Q59ZV4; -.
DR   ESTHER; canal-bna7; Kynurenine-formamidase.
DR   GeneID; 3643309; -.
DR   KEGG; cal:CAALFM_C114270WA; -.
DR   CGD; CAL0000192193; orf19.7237.
DR   VEuPathDB; FungiDB:C1_14270W_A; -.
DR   eggNOG; ENOG502S28Q; Eukaryota.
DR   HOGENOM; CLU_016852_1_0_1; -.
DR   InParanoid; Q59ZV4; -.
DR   OMA; NARWPDH; -.
DR   OrthoDB; 992858at2759; -.
DR   UniPathway; UPA00333; UER00454.
DR   Proteomes; UP000000559; Chromosome 1.
DR   GO; GO:0004061; F:arylformamidase activity; IBA:GO_Central.
DR   GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-UniRule.
DR   GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   HAMAP; MF_03014; KFase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   InterPro; IPR027519; KFase_ver/fungi-typ.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome; Tryptophan catabolism.
FT   CHAIN           1..267
FT                   /note="Kynurenine formamidase"
FT                   /id="PRO_0000361881"
FT   MOTIF           37..41
FT                   /note="HGGXW"
FT   ACT_SITE        104
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
FT   ACT_SITE        218
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
FT   ACT_SITE        250
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
SQ   SEQUENCE   267 AA;  30609 MW;  4E1B92AE06554649 CRC64;
     MEDISEEQEF KYGEHSLQKI KVFKYSSTNA STYIYIHGGA WRDPSNTFDE MRPVLGIPNA
     NLIGINYRLS PEIKHPEHLI DILRALRFVK QNFDVSQITL LGHSVGATMI LQLLHYRQII
     RDGLKHTHKD DLSSLDNLFA YVNDNVLLSQ VIFLDGIYDV VELLKEYPDY ASFVDDAFVS
     NKHFADSTQL SSANESLDLP FSLVSKDTKF LIYQSLEDDL LSMKQTHLLI DYLSSKNQGF
     TLHVGNWGKH EEIFGKYREI VFSGNVP
 
 
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