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Database: UniProt
Entry: Q2UIJ1_ASPOR
LinkDB: Q2UIJ1_ASPOR
Original site: Q2UIJ1_ASPOR 
ID   Q2UIJ1_ASPOR            Unreviewed;       349 AA.
AC   Q2UIJ1;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   24-JAN-2024, entry version 76.
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=AO090023000036 {ECO:0000313|EMBL:BAE58624.1};
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE58624.1, ECO:0000313|Proteomes:UP000006564};
RN   [1] {ECO:0000313|EMBL:BAE58624.1, ECO:0000313|Proteomes:UP000006564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007157; BAE58624.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2UIJ1; -.
DR   STRING; 510516.Q2UIJ1; -.
DR   EnsemblFungi; BAE58624; BAE58624; AO090023000036.
DR   HOGENOM; CLU_026207_2_0_1; -.
DR   OMA; FGFGECR; -.
DR   OrthoDB; 275827at2759; -.
DR   UniPathway; UPA00139; UER00341.
DR   Proteomes; UP000006564; Chromosome 3.
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: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:UP000006564};
KW   Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878,
KW   ECO:0000256|RuleBase:RU366008}.
FT   DOMAIN          10..108
FT                   /note="Fumarylacetoacetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09298"
FT   DOMAIN          114..343
FT                   /note="Fumarylacetoacetase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01557"
SQ   SEQUENCE   349 AA;  38653 MW;  09D1E3AB4B3D141B CRC64;
     MKATTPFPIE NLPYGVISTP SEPTPRCATA FEDYAIDLNE LQRDGFFDSI PGMIDGAFSK
     PALNVFASTP QSTQVEVRAR LVRFLPSASE ADKEKYFIRL SQVTNHLPME TANFSDFYCS
     LEHARNCSEI MGLEVNPNWY YIPSVYNGRT SSLRVSGQPI RRPWGVISGP GASSQATWSR
     SKRLDFELEM GVFLAKPLPA GQILDIRNAK EHVFGFVILN DWSARDIQGF EMAPLGPFHS
     KGFGTTISPW IVTIEALSPV ECPVSIPQSP PPLPHLAWKG DSSNATWDIE LSARILRKGK
     TYHITSTNLK DLYWTPYQQL THLASAGEGL STGDIFGTGT ISNDINYVN
//
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