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Database: UniProt
Entry: A0A194W123_9PEZI
LinkDB: A0A194W123_9PEZI
Original site: A0A194W123_9PEZI 
ID   A0A194W123_9PEZI        Unreviewed;       435 AA.
AC   A0A194W123;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Fumarylacetoacetase {ECO:0000256|ARBA:ARBA00012094, ECO:0000256|RuleBase:RU366008};
DE            EC=3.7.1.2 {ECO:0000256|ARBA:ARBA00012094, ECO:0000256|RuleBase:RU366008};
DE   AltName: Full=Fumarylacetoacetate hydrolase {ECO:0000256|RuleBase:RU366008};
GN   ORFNames=VM1G_05259 {ECO:0000313|EMBL:KUI69972.1};
OS   Valsa mali.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI69972.1};
RN   [1] {ECO:0000313|EMBL:KUI69972.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03-8 {ECO:0000313|EMBL:KUI69972.1};
RA   Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA   Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT   "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT   Colonization on Woody Bark.";
RL   Submitted (DEC-2014) 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|ARBA:ARBA00004782, ECO:0000256|RuleBase:RU366008}.
CC   -!- SIMILARITY: Belongs to the FAH family. {ECO:0000256|ARBA:ARBA00010211,
CC       ECO:0000256|RuleBase:RU366008}.
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DR   EMBL; CM003102; KUI69972.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A194W123; -.
DR   OrthoDB; 275827at2759; -.
DR   UniPathway; UPA00139; UER00341.
DR   Proteomes; UP000078559; Chromosome 5.
DR   GO; GO:0004334; F:fumarylacetoacetase activity; IEA:UniProtKB-UniRule.
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; 2.30.30.230; Fumarylacetoacetase, N-terminal domain; 1.
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   InterPro; IPR015377; Fumarylacetoacetase_N.
DR   InterPro; IPR036462; Fumarylacetoacetase_N_sf.
DR   NCBIfam; TIGR01266; fum_ac_acetase; 1.
DR   PANTHER; PTHR43069; FUMARYLACETOACETASE; 1.
DR   PANTHER; PTHR43069:SF2; FUMARYLACETOACETASE; 1.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   Pfam; PF09298; FAA_hydrolase_N; 1.
DR   SUPFAM; SSF56529; FAH; 1.
DR   SUPFAM; SSF63433; Fumarylacetoacetate hydrolase, FAH, N-terminal domain; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|RuleBase:RU366008};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366008};
KW   Magnesium {ECO:0000256|RuleBase:RU366008};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU366008};
KW   Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232,
KW   ECO:0000256|RuleBase:RU366008};
KW   Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878,
KW   ECO:0000256|RuleBase:RU366008}.
FT   DOMAIN          20..130
FT                   /note="Fumarylacetoacetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09298"
FT   DOMAIN          160..420
FT                   /note="Fumarylacetoacetase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01557"
SQ   SEQUENCE   435 AA;  47535 MW;  FF895D62AFD620D8 CRC64;
     MASFTTWVPG VEPDSDFSLA NIPFGIATTP HDSNPHAVTA IGSHVLDLKV LLGHPGAESI
     FACLKGHEHV ISSTSLNAFA ELGRDVHRQV RSSIQELLSV DTKQPEFLKE NTSLREKALI
     PLKDVKMSLP MRIGDYTDFY AGYHHAFGVG SMWRGPANAL QPNYTHLPVG YHGRASSIVV
     SGHPIKRPVG QVIVDPSAEL KQPVVKPSQK LDIELELGCF IARGNEMGTP IDVNQAEDHI
     FGYVLLNDWS ARDIQNWEYV PLGPFNGKNF STTISPWVIV PEALEPFKSR GIDLEGRPAL
     QDYLKEEKVD GFFDIKCEID LTTPEGDTTT ISKVSTKNLL WSFPQMLAHH TLGGCPMRSG
     DLIASGTISG TKPSEYGSLL EMSEGGKKEV LLYGMDARKF LKDGDTITFR ASGGESGNRV
     GFGECAGRIY SVVAR
//
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