ID A0A166QN47_9PEZI Unreviewed; 280 AA.
AC A0A166QN47;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Fumarylacetoacetase {ECO:0000256|RuleBase:RU366008};
DE EC=3.7.1.2 {ECO:0000256|RuleBase:RU366008};
DE AltName: Full=Fumarylacetoacetate hydrolase {ECO:0000256|RuleBase:RU366008};
GN ORFNames=CT0861_03951 {ECO:0000313|EMBL:KZL68142.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL68142.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL68142.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL68142.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-fumarylacetoacetate + H2O = acetoacetate + fumarate + H(+);
CC Xref=Rhea:RHEA:10244, ChEBI:CHEBI:13705, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18034, ChEBI:CHEBI:29806; EC=3.7.1.2;
CC Evidence={ECO:0000256|RuleBase:RU366008};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU366008};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|RuleBase:RU366008};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 6/6.
CC {ECO:0000256|RuleBase:RU366008}.
CC -!- SIMILARITY: Belongs to the FAH family. {ECO:0000256|ARBA:ARBA00010211,
CC ECO:0000256|RuleBase:RU366008}.
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:KZL68142.1}.
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DR EMBL; LFIV01000128; KZL68142.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166QN47; -.
DR STRING; 708197.A0A166QN47; -.
DR OrthoDB; 275827at2759; -.
DR UniPathway; UPA00139; UER00341.
DR Proteomes; UP000076552; Unassembled WGS sequence.
DR GO; GO:0004334; F:fumarylacetoacetase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.850.10; Fumarylacetoacetase-like, C-terminal domain; 1.
DR InterPro; IPR005959; Fumarylacetoacetase.
DR InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR PANTHER; PTHR43069; FUMARYLACETOACETASE; 1.
DR PANTHER; PTHR43069:SF2; FUMARYLACETOACETASE; 1.
DR Pfam; PF01557; FAA_hydrolase; 1.
DR SUPFAM; SSF56529; FAH; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|RuleBase:RU366008};
KW Hydrolase {ECO:0000256|RuleBase:RU366008};
KW Isomerase {ECO:0000313|EMBL:KZL68142.1};
KW Magnesium {ECO:0000256|RuleBase:RU366008};
KW Metal-binding {ECO:0000256|RuleBase:RU366008};
KW Phenylalanine catabolism {ECO:0000256|RuleBase:RU366008};
KW Reference proteome {ECO:0000313|Proteomes:UP000076552};
KW Tyrosine catabolism {ECO:0000256|RuleBase:RU366008}.
FT DOMAIN 12..279
FT /note="Fumarylacetoacetase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01557"
SQ SEQUENCE 280 AA; 30327 MW; 693447EBD0B15CA1 CRC64;
MGAFPGHDEV PSNSYHIPLA YNGRASSVVI SGVPIIRPWG YIPTPDGPKF QPTQKMDFEV
EMGIFIAKPL DIGEAVPASQ ARDHIFGMVL LNDWSARDIK FYEMVPLGPF NGKACGTSIS
PWIVTLDALE EAGAVIDVEA GKLPGGKWAK DSFLAYSRDV SVQVTTHISR MAAQKPSFPQ
QWRHSKSLFA QSKLKHLHWS PLQMVAHQSS AGCGLNSGDL LCTGTMSSTE QQASEDGVLA
GTGRSGCLQE ATKNAKHPLP LENGQKLIWI EDGDEVVMEA
//
