FAAA_RAT
ID FAAA_RAT Reviewed; 419 AA.
AC P25093;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 136.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=1916290; DOI=10.1016/0378-1119(91)90250-f;
RA Labelle Y., Phaneuf D., Tanguay R.M.;
RT "Cloning and expression analysis of a cDNA encoding fumarylacetoacetate
RT hydrolase: post-transcriptional modulation in rat liver and kidney.";
RL Gene 104:197-202(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 32-47; 145-162 AND 382-402, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-92 AND SER-417, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- TISSUE SPECIFICITY: Mainly in liver and kidney.
CC {ECO:0000269|PubMed:1916290}.
CC -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
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DR EMBL; M77694; AAA41142.1; -; mRNA.
DR EMBL; BC076381; AAH76381.1; -; mRNA.
DR PIR; JH0467; JH0467.
DR RefSeq; NP_058877.1; NM_017181.2.
DR AlphaFoldDB; P25093; -.
DR SMR; P25093; -.
DR STRING; 10116.ENSRNOP00000061132; -.
DR iPTMnet; P25093; -.
DR PhosphoSitePlus; P25093; -.
DR PRIDE; P25093; -.
DR Ensembl; ENSRNOT00000068167; ENSRNOP00000061132; ENSRNOG00000013223.
DR GeneID; 29383; -.
DR KEGG; rno:29383; -.
DR UCSC; RGD:61932; rat.
DR CTD; 2184; -.
DR RGD; 61932; Fah.
DR eggNOG; KOG2843; Eukaryota.
DR GeneTree; ENSGT00390000008646; -.
DR InParanoid; P25093; -.
DR OrthoDB; 980065at2759; -.
DR PhylomeDB; P25093; -.
DR Reactome; R-RNO-8963684; Tyrosine catabolism.
DR UniPathway; UPA00139; UER00341.
DR PRO; PR:P25093; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0004334; F:fumarylacetoacetase activity; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006527; P:arginine catabolic process; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Calcium; Direct protein sequencing; Hydrolase;
KW Lipid metabolism; Magnesium; Metal-binding; Phenylalanine catabolism;
KW Phosphoprotein; 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_0000156827"
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 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16930"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 419 AA; 45976 MW; AC099689591C6176 CRC64;
MSFIPVAEDS DFPIQNLPYG VFSTQSNPKP RIGVAIGDQI LDLSVIKHLF TGPVLSKHQH
VFDETTLNSF MGLGQAAWKE ARASLQNLLS ASQAQLRDDK ELRQRAFTSQ ASATMHLPAT
IGDYTDFYSS LQHATNVGIM FRGKENALLP NWLHLPVGYH GRASSVVVSG TPIRRPMGQM
RPDNSKPPVY GASKRLDMEL EMAFFVGPGN RFGEPIPISK AQEHIFGMVL MNDWSARDIQ
QWEYVPLGPF LGKSFGTTIS PWVVPMDALM PFVVPNPKQD PKPLPYLCHS QPYTFDINLS
VALKGEGMSQ AATICRSNFK HMYWTILQQL THHSVNGCNL RPGDLLASGT ISGSDPESFG
SMLELSWKGT KAIDVGQGQT RTFLLDGDEV IITGHCQGDG YRVGFGQCAG KVLPALSPA
