ID A0A0D2E3C3_9EURO Unreviewed; 1014 AA.
AC A0A0D2E3C3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=fumarylacetoacetase {ECO:0000256|ARBA:ARBA00012094};
DE EC=3.7.1.2 {ECO:0000256|ARBA:ARBA00012094};
GN ORFNames=PV05_10973 {ECO:0000313|EMBL:KIW49280.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW49280.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW49280.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW49280.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 6/6.
CC {ECO:0000256|ARBA:ARBA00004782}.
CC -!- SIMILARITY: Belongs to the FAH family. {ECO:0000256|ARBA:ARBA00010211}.
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DR EMBL; KN847323; KIW49280.1; -; Genomic_DNA.
DR RefSeq; XP_013309864.1; XM_013454410.1.
DR AlphaFoldDB; A0A0D2E3C3; -.
DR STRING; 348802.A0A0D2E3C3; -.
DR GeneID; 25332881; -.
DR HOGENOM; CLU_297181_0_0_1; -.
DR OrthoDB; 2314924at2759; -.
DR UniPathway; UPA00139; UER00341.
DR Proteomes; UP000054342; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004334; F:fumarylacetoacetase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-KW.
DR CDD; cd12148; fungal_TF_MHR; 1.
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 InterPro; IPR007219; Transcription_factor_dom_fun.
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 Pfam; PF04082; Fungal_trans; 1.
DR SMART; SM00906; Fungal_trans; 1.
DR SUPFAM; SSF56529; FAH; 1.
DR SUPFAM; SSF63433; Fumarylacetoacetate hydrolase, FAH, N-terminal domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232};
KW Reference proteome {ECO:0000313|Proteomes:UP000054342};
KW Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878}.
FT DOMAIN 704..777
FT /note="Transcription factor"
FT /evidence="ECO:0000259|SMART:SM00906"
FT REGION 441..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1014 AA; 113097 MW; 5525965619681D2A CRC64;
MVLKTWLDVP DEHDFSVENL PFGIFSTAAN TRPRPGIAIG RFIVDLDALV ETEAFSMYCT
CQFPHSVLKQ STLNEFAALG RETVNAVRIF VKYLLVEMTP ILRDDKALRA NCIVDTEAVR
VEMHLPMQIG DFTDFLNSRT HAKNTHSTSA APVNMLVAYH NKFNPPRAFT ARVSSVVPSG
TPIVRPMGHM VDSDGKAYVG PSQQLDVEME FAFFLGKAIK RYQRVSIAEA EDHIFGVVLL
NDWSTRDVQA FEDHPFAAFN AKSFASTISP WVVSLDALEH YRTKAAPQDP SDLLPYLTDS
RALSTFDISI NMSWKLSPEG EIFNVSTSNL TNAYWSFTQM LTHHAFGGCE MRTGDLIGTG
TITGEDDGSI CSLVERTRNG TQQIQTPAGN RRCYVQDGDE VVFTGWAAKK GDPKLAGGRV
GFGIYTQSAP PPVNDFDLAL LFSPQSNNDG SPHRSPAEAG GSVASQASLE SNDNTDLPRR
LQGRGNTSET LDGWPATTTF LLGDTGESDP YLLRHFSSEC LDSSDDIAKV TSRHILRASD
PDVMHSMGRP LIMSMADHSL YDRGEPRLDQ RALDEAADEV SRMVSEETGV RLIKLFFRYI
YPYFPILSRT RLLYPLTELP ARLRELPLSL KSAIYASALA FVTYDDVLAT TLVHSPPSSQ
RLYRIAWLAV THEVHTPHLS TLQSCLLLLQ RVNDDRYVMD TVFRWSLLGW TVALAQSFGL
SIDCLDWNGI PDWEKRLRRR LWWAVFVMDK WAFMSAGLTS HIHKDNYDVS PLTTADFGYA
ETPEPTSSDN TSAHFYHLTR LTAILSDIQV AFFTVAASKR TQRDFALSIE LAKPFRQDLK
EWKTSYDSFI ATQAASRDQS RSLRSGLDGN ASLGLSYLVA NIILFRALLR PVESNLPSTN
QQPRAGRDAV RAGAKTCCVE AVAFVESLQR NVWDAFWHSW SRAGFAMVSS LMIRLLITSD
KAIEVDEINA LIRRWRWALR TGGGSAGNVL MSLALLRLDR SLVTRGIHES DEDE
//
