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Database: UniProt
Entry: A0A397UCQ6_9GLOM
LinkDB: A0A397UCQ6_9GLOM
Original site: A0A397UCQ6_9GLOM 
ID   A0A397UCQ6_9GLOM        Unreviewed;       275 AA.
AC   A0A397UCQ6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   22-FEB-2023, entry version 10.
DE   RecName: Full=Kynurenine formamidase {ECO:0000256|HAMAP-Rule:MF_03014};
DE            Short=KFA {ECO:0000256|HAMAP-Rule:MF_03014};
DE            Short=KFase {ECO:0000256|HAMAP-Rule:MF_03014};
DE            EC=3.5.1.9 {ECO:0000256|HAMAP-Rule:MF_03014};
DE   AltName: Full=Arylformamidase {ECO:0000256|HAMAP-Rule:MF_03014};
DE   AltName: Full=N-formylkynurenine formamidase {ECO:0000256|HAMAP-Rule:MF_03014};
DE            Short=FKF {ECO:0000256|HAMAP-Rule:MF_03014};
GN   ORFNames=C2G38_2115107 {ECO:0000313|EMBL:RIB06857.1};
OS   Gigaspora rosea.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Diversisporales; Gigasporaceae; Gigaspora.
OX   NCBI_TaxID=44941 {ECO:0000313|EMBL:RIB06857.1, ECO:0000313|Proteomes:UP000266673};
RN   [1] {ECO:0000313|EMBL:RIB06857.1, ECO:0000313|Proteomes:UP000266673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM 194757 {ECO:0000313|EMBL:RIB06857.1,
RC   ECO:0000313|Proteomes:UP000266673};
RA   Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA   Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA   Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT   "Comparative genomics reveals the genomic features of Rhizophagus
RT   irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT   symbiotic lifestyle signature.";
RL   Submitted (JUN-2018) 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. Kynurenine may be further oxidized to nicotinic acid,
CC       NAD(H) and NADP(H). Required for elimination of toxic metabolites.
CC       {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_03014}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|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:0000256|HAMAP-
CC       Rule:MF_03014}.
CC   -!- SIMILARITY: Belongs to the kynurenine formamidase family.
CC       {ECO:0000256|HAMAP-Rule:MF_03014}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RIB06857.1}.
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DR   EMBL; QKWP01001751; RIB06857.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397UCQ6; -.
DR   STRING; 44941.A0A397UCQ6; -.
DR   UniPathway; UPA00333; UER00454.
DR   Proteomes; UP000266673; Unassembled WGS sequence.
DR   GO; GO:0004061; F:arylformamidase activity; IEA:UniProtKB-UniRule.
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; alpha/beta hydrolase; 1.
DR   HAMAP; MF_03014; KFase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR027519; KFase_ver/fungi-typ.
DR   PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR   PANTHER; PTHR48081:SF8; KYNURENINE FORMAMIDASE; 1.
DR   Pfam; PF20434; BD-FAE; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03014};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266673};
KW   Tryptophan catabolism {ECO:0000256|ARBA:ARBA00023079, ECO:0000256|HAMAP-
KW   Rule:MF_03014}.
FT   MOTIF           46..50
FT                   /note="HGGXW"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
FT   ACT_SITE        122
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
FT   ACT_SITE        211
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
FT   ACT_SITE        247
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
SQ   SEQUENCE   275 AA;  31352 MW;  242812797260ADB9 CRC64;
     MNQEKCELIL HADIPYSSHP QQTLDLYIHS LIANTKLLTP IIIMIHGGAW ITGDKEDLKP
     LGKFISSLTN FAVALINYRI SNTPEIKHPM HINDVAAAIS WIYSNCDKYG YRNDSMYLVG
     HSVGAFLSAQ LIFIPEYRTK ELLNSIRGVV GIEGIYDIPT LLERWPDYTR YVEPAFGTDP
     KVYKSASPQY HSIKDEATII PPYLIIHSLE DELVDIGQAN DFYKYVEQIC KTNESYVELE
     TGIKGTHDGI LNKRELEQRI VEFILLRQAK LSFSE
//
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