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Database: UniProt
Entry: G0RIP5_HYPJQ
LinkDB: G0RIP5_HYPJQ
Original site: G0RIP5_HYPJQ 
ID   G0RIP5_HYPJQ            Unreviewed;       432 AA.
AC   G0RIP5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 46.
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=TRIREDRAFT_77749 {ECO:0000313|EMBL:EGR49245.1};
OS   Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN   [1] {ECO:0000313|EMBL:EGR49245.1, ECO:0000313|Proteomes:UP000008984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QM6a {ECO:0000313|EMBL:EGR49245.1,
RC   ECO:0000313|Proteomes:UP000008984};
RX   PubMed=18454138; DOI=10.1038/nbt1403;
RA   Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA   Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA   Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA   Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA   Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA   Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA   Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA   Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT   "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT   reesei (syn. Hypocrea jecorina).";
RL   Nat. Biotechnol. 26:553-560(2008).
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; GL985063; EGR49245.1; -; Genomic_DNA.
DR   RefSeq; XP_006965205.1; XM_006965143.1.
DR   AlphaFoldDB; G0RIP5; -.
DR   STRING; 431241.G0RIP5; -.
DR   EnsemblFungi; EGR49245; EGR49245; TRIREDRAFT_77749.
DR   GeneID; 18488805; -.
DR   KEGG; tre:TRIREDRAFT_77749; -.
DR   VEuPathDB; FungiDB:TRIREDRAFT_77749; -.
DR   eggNOG; KOG2843; Eukaryota.
DR   HOGENOM; CLU_026207_2_0_1; -.
DR   OrthoDB; 275827at2759; -.
DR   UniPathway; UPA00139; UER00341.
DR   Proteomes; UP000008984; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000008984};
KW   Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878,
KW   ECO:0000256|RuleBase:RU366008}.
FT   DOMAIN          19..129
FT                   /note="Fumarylacetoacetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09298"
FT   DOMAIN          143..423
FT                   /note="Fumarylacetoacetase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01557"
SQ   SEQUENCE   432 AA;  47192 MW;  98ECB1220882D2F6 CRC64;
     MASLTSWVPL DRNGDFSIHN LPFGIFSDAG SSQPRAGTRI GDFVLDLSAL AGDAQVKQQL
     GSFSGLEGVF SQTSLNAFAE RGRAVHRAVR ADLQRLLSES TDVPALLKDN EALKQKALVP
     VDKVTMHLPM QIGDYTDFYA GYHHAYKVGV LFRGPDNALQ PNYTHLPVGY HGRSSSIVVS
     GTPIRRPRGQ ILPNPAATPK QPTTVPCRRL DFELELGCFI SKPNEMGDPI DISKAEEYIF
     GFVLLNDWSA RDIQAWEYVP LGPFNGKNFG STISPWVVVP DALEPFRTEP LQNDTPIQDY
     LKETQKQSVF DIQLEVGLTT ADGDHVDLTK TSGRNLLWSF PQMIAHHTVG GCPLRAGDLL
     GSGTISGTEP RERGSLLEMT EGGKADVQLE KGGVRRFIED GDSVNMRGYC EKNGVRIGFG
     DCEGKILPAH GS
//
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