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Database: UniProt
Entry: S0EBF5_GIBF5
LinkDB: S0EBF5_GIBF5
Original site: S0EBF5_GIBF5 
ID   S0EBF5_GIBF5            Unreviewed;       412 AA.
AC   S0EBF5;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=FFUJ_08888 {ECO:0000313|EMBL:CCT71072.1};
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS   and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT71072.1, ECO:0000313|Proteomes:UP000016800};
RN   [1] {ECO:0000313|Proteomes:UP000016800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC   {ECO:0000313|Proteomes:UP000016800};
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA   Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA   Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA   Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA   Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT   Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT   novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(2013).
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; HF679029; CCT71072.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0EBF5; -.
DR   STRING; 1279085.S0EBF5; -.
DR   EnsemblFungi; CCT71072; CCT71072; FFUJ_08888.
DR   VEuPathDB; FungiDB:FFUJ_08888; -.
DR   HOGENOM; CLU_026207_2_0_1; -.
DR   OrthoDB; 275827at2759; -.
DR   UniPathway; UPA00139; UER00341.
DR   Proteomes; UP000016800; Chromosome 7.
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   PANTHER; PTHR43069; FUMARYLACETOACETASE; 1.
DR   PANTHER; PTHR43069:SF5; 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:UP000016800};
KW   Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878,
KW   ECO:0000256|RuleBase:RU366008}.
FT   DOMAIN          13..111
FT                   /note="Fumarylacetoacetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09298"
FT   DOMAIN          117..388
FT                   /note="Fumarylacetoacetase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01557"
FT   REGION          344..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   412 AA;  44394 MW;  DDF0255A949C53C5 CRC64;
     MAATDFAHHF TEKNIPFGIA SSESHNTPQA VTRLGNTVIF LSDLVEQLFK DVEGLSRGVF
     NEETLNSFAA LPKTVHQNVR KQIQQAHRHK GLDGFPTSSK EDITAVTMHL PVEIKDFADF
     SCSLDHVINA GRIVVNNGTP PPGFFKFPVG YQGRTGSIVV SGTDIERPYG QFKNPAAAEG
     DDPITYAPSQ KVDYEVELAA VVGKPLAMRQ RLHAKDAEEH IFGFVILNDW SARDIQGFEM
     FPLGPFNGKS LGTSISPWII TLDALEPFRT KAQEQKAISA SYLQHPSPST FSITLKVDVL
     ANNTTTTLGV CPVESLYWTP QQMVAHSVSS GSALRTGDLL ATGTVSGSEE TSRGCMLEST
     EGGTKPVTLS DGSKRGFLED GDVVRITGSV GGDESGVGFG ECIGKLTPAR SY
//
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