ID G9MP47_HYPVG Unreviewed; 431 AA.
AC G9MP47;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=TRIVIDRAFT_79823 {ECO:0000313|EMBL:EHK23649.1};
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK23649.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK23649.1, ECO:0000313|Proteomes:UP000007115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
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}.
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:EHK23649.1}.
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DR EMBL; ABDF02000005; EHK23649.1; -; Genomic_DNA.
DR RefSeq; XP_013957861.1; XM_014102386.1.
DR AlphaFoldDB; G9MP47; -.
DR STRING; 413071.G9MP47; -.
DR EnsemblFungi; EHK23649; EHK23649; TRIVIDRAFT_79823.
DR GeneID; 25798118; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_79823; -.
DR eggNOG; KOG2843; Eukaryota.
DR HOGENOM; CLU_026207_2_0_1; -.
DR InParanoid; G9MP47; -.
DR OMA; FIELTWG; -.
DR OrthoDB; 275827at2759; -.
DR UniPathway; UPA00139; UER00341.
DR Proteomes; UP000007115; 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:UP000007115};
KW Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878,
KW ECO:0000256|RuleBase:RU366008}.
FT DOMAIN 19..128
FT /note="Fumarylacetoacetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09298"
FT DOMAIN 142..420
FT /note="Fumarylacetoacetase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01557"
SQ SEQUENCE 431 AA; 47407 MW; 4E021B1A600A26FC CRC64;
MTSQTSWVPV DKNGDFSIHN LPFGIFSEGS SLPRAASRIG DFVIDLKALA GDEQAKQQLT
SLRDLEGVFG QTSLNAFAER GRAVHRAVRA DLQRILSQST DLPAILKDNE SLKQKVLIPV
EKVKMHLPMQ IGDYTDFYAG YHHAYKVGVL FRGPDNALQP NYTHLPVGYH GRSSSIVVSG
TPIRRPRGQI LPNPAATPKE PTTVPCRRLD FELELGCFIC KPNEMGESID INNAEEYIFG
FVLLNDWSAR DIQAWEYVPL GPFNGKNFGS TISPWVVVAD ALEPFRTEPL ANDTPVQDYL
KETQKKSVFD IQLEVGLTTA DGDHVDLTKT SGRNLLWSFP QMITHHTVGG CPLRAGDLLG
SGTISGTEPR ERGSLLEMTE GGKVDVQLEK GGVRRFIQDG DSLNMRGYCE KDGVRIGFGD
CEGKILPAHG A
//
