ID   FAHD1_BOVIN             Reviewed;         221 AA.
AC   Q2HJ98;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Acylpyruvase FAHD1, mitochondrial;
DE            EC=3.7.1.5 {ECO:0000250|UniProtKB:Q6P587};
DE   AltName: Full=Fumarylacetoacetate hydrolase domain-containing protein 1;
DE   AltName: Full=Oxaloacetate decarboxylase {ECO:0000250|UniProtKB:Q6P587};
DE            Short=OAA decarboxylase {ECO:0000250|UniProtKB:Q6P587};
DE            EC=4.1.1.112 {ECO:0000250|UniProtKB:Q6P587};
DE   Flags: Precursor;
GN   Name=FAHD1;
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=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable mitochondrial acylpyruvase which is able to
CC       hydrolyze acetylpyruvate and fumarylpyruvate in vitro. Also has
CC       oxaloacetate decarboxylase activity. {ECO:0000250|UniProtKB:Q6P587}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3-acylpyruvate + H2O = a carboxylate + H(+) + pyruvate;
CC         Xref=Rhea:RHEA:19009, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:57278; EC=3.7.1.5;
CC         Evidence={ECO:0000250|UniProtKB:Q6P587};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:16526; EC=4.1.1.112;
CC         Evidence={ECO:0000250|UniProtKB:Q6P587};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q6P587};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q6P587};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6P587}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q6P587}.
CC       Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q6P587}.
CC   -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
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DR   EMBL; BC113240; AAI13241.1; -; mRNA.
DR   RefSeq; NP_001068868.1; NM_001075400.1.
DR   AlphaFoldDB; Q2HJ98; -.
DR   SMR; Q2HJ98; -.
DR   STRING; 9913.ENSBTAP00000044120; -.
DR   PaxDb; Q2HJ98; -.
DR   Ensembl; ENSBTAT00000046873; ENSBTAP00000044120; ENSBTAG00000033015.
DR   GeneID; 509273; -.
DR   KEGG; bta:509273; -.
DR   CTD; 81889; -.
DR   VEuPathDB; HostDB:ENSBTAG00000033015; -.
DR   VGNC; VGNC:28708; FAHD1.
DR   eggNOG; KOG1535; Eukaryota.
DR   GeneTree; ENSGT00940000160452; -.
DR   HOGENOM; CLU_028458_5_0_1; -.
DR   InParanoid; Q2HJ98; -.
DR   OMA; YALSIDM; -.
DR   OrthoDB; 1216556at2759; -.
DR   TreeFam; TF300911; -.
DR   Reactome; R-BTA-71403; Citric acid cycle (TCA cycle).
DR   Proteomes; UP000009136; Chromosome 25.
DR   Bgee; ENSBTAG00000033015; Expressed in longissimus thoracis muscle and 108 other tissues.
DR   ExpressionAtlas; Q2HJ98; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0018773; F:acetylpyruvate hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0047621; F:acylpyruvate hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034545; F:fumarylpyruvate hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; ISS:UniProtKB.
DR   Gene3D; 3.90.850.10; -; 1.
DR   InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR   InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   SUPFAM; SSF56529; SSF56529; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Calcium; Cytoplasm; Hydrolase; Lyase; Magnesium;
KW   Metal-binding; Mitochondrion; Phosphoprotein; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..24
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..221
FT                   /note="Acylpyruvase FAHD1, mitochondrial"
FT                   /id="PRO_0000285513"
FT   BINDING         68
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P587"
FT   BINDING         70
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P587"
FT   BINDING         99
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P587"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6AYQ8"
FT   MOD_RES         110
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R0F8"
FT   MOD_RES         112
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R0F8"
SQ   SEQUENCE   221 AA;  24499 MW;  465D9C5904E06AD8 CRC64;
     MAASRPLSRF WEWGKNIVCV GRNYADHVRE MQSAAPSEPV LFLKPSTAYA PEGSPVLVPA
     YTRNLHHELE LAVVMGKRCR AVSEAAAMDY VAGYALCLDM TARDVQDECK KKGLPWTLAK
     SFTASCPVSA FVPKEKIPDP HNLKLWLKVN GELRQEGETS SMIFSIPYII SYVSKIMTLE
     EGDIILTGTP KGVGPVKEND EIQAGIHGVL SMKFKVERPE Y