FAHD1_RAT
ID FAHD1_RAT Reviewed; 221 AA.
AC Q6AYQ8;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Acylpyruvase FAHD1, mitochondrial;
DE EC=3.7.1.5;
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 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 [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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION BY
RP 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 -!- 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 -!- 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; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Cytoplasm, cytosol
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
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DR EMBL; BC078950; AAH78950.1; -; mRNA.
DR RefSeq; NP_001020162.1; NM_001024991.1.
DR AlphaFoldDB; Q6AYQ8; -.
DR SMR; Q6AYQ8; -.
DR STRING; 10116.ENSRNOP00000019767; -.
DR iPTMnet; Q6AYQ8; -.
DR PhosphoSitePlus; Q6AYQ8; -.
DR jPOST; Q6AYQ8; -.
DR PaxDb; Q6AYQ8; -.
DR PRIDE; Q6AYQ8; -.
DR Ensembl; ENSRNOT00000019767; ENSRNOP00000019767; ENSRNOG00000014727.
DR GeneID; 302980; -.
DR KEGG; rno:302980; -.
DR UCSC; RGD:1304560; rat.
DR CTD; 81889; -.
DR RGD; 1304560; Fahd1.
DR eggNOG; KOG1535; Eukaryota.
DR GeneTree; ENSGT00940000160452; -.
DR HOGENOM; CLU_028458_5_0_1; -.
DR InParanoid; Q6AYQ8; -.
DR OMA; YALSIDM; -.
DR OrthoDB; 1216556at2759; -.
DR PhylomeDB; Q6AYQ8; -.
DR Reactome; R-RNO-71403; Citric acid cycle (TCA cycle).
DR PRO; PR:Q6AYQ8; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000014727; Expressed in kidney and 20 other tissues.
DR Genevisible; Q6AYQ8; RN.
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 1: Evidence at protein 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_0000156832"
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:0007744|PubMed:22673903"
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; 24480 MW; 1CFBC9984C611D09 CRC64;
MASTKPLSRF WEWGKNIVCV GRNYADHVKE MRSTVLSEPV LFLKPSTAYA PEGSPVLMPA
YCRNLHHEVE LGVLLGRRGE AVPEAAAMDY VAGYALCLDM TARDVQDECK KKGLPWTLAK
SFTSSCPVSA FVPKEKIPDP HALRLWLKVN GELRQEGKTS SMIFSIPYII SYVSKIITLE
EGDLILTGTP KGVGAVKEND EIEAGIDGVV SMRFKVERSK Y
