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Database: UniProt
Entry: K9J0Q2_DESRO
LinkDB: K9J0Q2_DESRO
Original site: K9J0Q2_DESRO 
ID   K9J0Q2_DESRO            Unreviewed;       419 AA.
AC   K9J0Q2;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Fumarylacetoacetase {ECO:0000256|ARBA:ARBA00014741, 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};
OS   Desmodus rotundus (Vampire bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Phyllostomidae;
OC   Desmodontinae; Desmodus.
OX   NCBI_TaxID=9430 {ECO:0000313|EMBL:JAA47234.1};
RN   [1] {ECO:0000313|EMBL:JAA47234.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Salivary gland {ECO:0000313|EMBL:JAA47234.1};
RA   Francischetti I.M.B., Assumpcao T.C.F., Ma D., Vicente E.C.,
RA   Ribeiro J.M.C.;
RT   "The Vampirome: Transcriptome and Proteome Analysis of the Submandibular
RT   and Accessory Glands of the Vampire Bat and Vector of Human Rabies,
RT   Desmodus rotundus.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000353,
CC         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; GABZ01006291; JAA47234.1; -; mRNA.
DR   AlphaFoldDB; K9J0Q2; -.
DR   OrthoDB; 275827at2759; -.
DR   UniPathway; UPA00139; UER00341.
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   2: Evidence at transcript level;
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   Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878,
KW   ECO:0000256|RuleBase:RU366008}.
FT   DOMAIN          15..118
FT                   /note="Fumarylacetoacetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09298"
FT   DOMAIN          125..399
FT                   /note="Fumarylacetoacetase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01557"
SQ   SEQUENCE   419 AA;  46273 MW;  4C17BC42F985590B CRC64;
     MSFVPVAKNS DFPIQNLPYG VFTTTGNLRP RIGVAIGDQI LDLSVIKHLF TGPVLSKHQD
     VFDQPTLNSF MGLGQAAWRE VRAFLQNLLS ASQARLRDDT ELRKRAFVSQ ASATMHLPAA
     IGDYTDFYSS RQHATNVGIM FRGKENALMP NWLHLPVGYH GRASSIVVSG TPIRRPLGQM
     RPDDSKPPVY GPCKLLDIEL EMAFFVGPGN KFGEPIPISK AHEHIFGMVL MNDWSARDIQ
     KWEYVPLGPF LGKSFGTTIS PWVVPMDALM PFVVPNPEQD PKPLPYLCHD QPYTFDIHLS
     VALKGEGMSQ AATICKSNFK YMHWTMLQQL THHSINGCNL RPGDLLASGT ISGPEPESFG
     SMLELSWRGT KAIELGNGQT RKFLQDGDEV IITGHCQGDG YRVGFGQCVG KVLPSLLPA
//
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