FAAA_BOVIN
ID FAAA_BOVIN Reviewed; 419 AA.
AC A5PKH3; A7MBC9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Fumarylacetoacetase;
DE Short=FAA;
DE EC=3.7.1.2 {ECO:0000250|UniProtKB:P35505};
DE AltName: Full=Beta-diketonase;
DE AltName: Full=Fumarylacetoacetate hydrolase;
GN Name=FAH;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon, Fetal liver, and Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2007) 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:0000250|UniProtKB:P35505};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P35505};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P35505};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 6/6.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P35505}.
CC -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
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DR EMBL; BC142487; AAI42488.1; -; mRNA.
DR EMBL; BC151490; AAI51491.1; -; mRNA.
DR EMBL; BC151824; AAI51825.1; -; mRNA.
DR RefSeq; NP_001092382.1; NM_001098912.1.
DR AlphaFoldDB; A5PKH3; -.
DR SMR; A5PKH3; -.
DR STRING; 9913.ENSBTAP00000016368; -.
DR PaxDb; A5PKH3; -.
DR PeptideAtlas; A5PKH3; -.
DR PRIDE; A5PKH3; -.
DR GeneID; 508724; -.
DR KEGG; bta:508724; -.
DR CTD; 2184; -.
DR eggNOG; KOG2843; Eukaryota.
DR InParanoid; A5PKH3; -.
DR OrthoDB; 980065at2759; -.
DR UniPathway; UPA00139; UER00341.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0004334; F:fumarylacetoacetase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1902000; P:homogentisate catabolic process; IBA:GO_Central.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006572; P:tyrosine catabolic process; IBA:GO_Central.
DR Gene3D; 2.30.30.230; -; 1.
DR Gene3D; 3.90.850.10; -; 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; PTHR43069; 1.
DR Pfam; PF01557; FAA_hydrolase; 1.
DR Pfam; PF09298; FAA_hydrolase_N; 1.
DR SUPFAM; SSF56529; SSF56529; 1.
DR SUPFAM; SSF63433; SSF63433; 1.
DR TIGRFAMs; TIGR01266; fum_ac_acetase; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Calcium; Hydrolase; Lipid metabolism; Magnesium;
KW Metal-binding; Phenylalanine catabolism; Phosphoprotein;
KW Reference proteome; Tyrosine catabolism.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P16930"
FT CHAIN 2..419
FT /note="Fumarylacetoacetase"
FT /id="PRO_0000318804"
FT ACT_SITE 133
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 257
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P16930"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16930"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25093"
FT CONFLICT 332
FT /note="H -> D (in Ref. 1; AAI51491)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 46156 MW; 801EA75E57B729DD CRC64;
MSFVPVAEDS DFPIHNLPYG VFSTRGNPRP RIGVAIGDQI LDLSVIKHLF TGPILSGHQD
VFNKPTLNSF MGLGQAAWKE ARAFLQNLLS ASQARLRDDV ELRQRAFTSQ ASATMYLPAT
IGDYTDFYSS RHHATNVGVM FRGKENALMP NWLHLPVGYH GRASSVVVSG TPIRRPLGQM
RPDDSKPPVY GACKLLDFEL EMAFFVGPGN KLGEPIPISK AHEHIFGMVL MNDWSARDIQ
KWEYVPLGPF LGKSFGTTIS PWVVPMDALM PFAVSNPEQD PKPLPYLCHD QPYTFDINLS
VALKGEGMSQ AATICRSNFK YMYWTMLQQL THHSVNGCNL QPGDLLASGT ISGPEPESFG
CMLELSWKGT RAVELGNGQT RKFLLDGDEV IMTGHCQGDG YRIGFGQCAG KVLPALSFA
