UniProt Accession

 FAHD1_MOUSE; Q8R0F8; Q3U020; Q3UQY4; Q8BLJ7; Q9JJB2 

Genbank Protein ID

 AB041600; AK044920; AK157292; AK141973; AC166102; BC026949 

Genbank Nucleotide ID

 BAA95083.1; BAC32142.1; BAE34035.1; BAE24904.1; AAH26949.1 

Protein Name

 Acylpyruvase FAHD1, mitochondrial 

Protein Synonyms/Alias

 Fumarylacetoacetate hydrolase domain-containing protein 1 

Gene Name

 Fahd1 

Gene Synonyms/Alias

 MNCb-4134 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
35	RNYADHVKEMRSTVL	acetylation	[1]
35	RNYADHVKEMRSTVL	succinylation	[1]
83	ELGVLLGKRGEAIPE	acetylation	[2, 3]
116	RDVQEECKKKGLPWT	acetylation	[2, 3, 4]
117	DVQEECKKKGLPWTL	acetylation	[4]
118	VQEECKKKGLPWTLA	acetylation	[1]
118	VQEECKKKGLPWTLA	succinylation	[1]
140	PVSAFVPKEKIPDPH	acetylation	[4]
142	SAFVPKEKIPDPHAL	acetylation	[2, 3, 4]

Reference

 [1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [2] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [3] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [4] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123] 

Functional Description

 Probable mitochondrial acylpyruvase which is able to hydrolyze acetylpyruvate and fumarylpyruvate in vitro (By similarity). 

Sequence Annotation

 METAL 74 74 Divalent metal cation (By similarity).
 METAL 76 76 Divalent metal cation (By similarity).
 METAL 105 105 Divalent metal cation (By similarity).  

Keyword

 Calcium; Complete proteome; Cytoplasm; Hydrolase; Magnesium; Metal-binding; Mitochondrion; Reference proteome; Transit peptide. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 227 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0018773; F:acetylpyruvate hydrolase activity; ISS:UniProtKB.
 GO:0047621; F:acylpyruvate hydrolase activity; IEA:EC.
 GO:0034545; F:fumarylpyruvate hydrolase activity; ISS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 

Interpro

 IPR002529; Fumarylacetoacetase_C.
 IPR011234; Fumarylacetoacetase_C-rel. 

Pfam

 PF01557; FAA_hydrolase 

SMART

  

PROSITE

  

PRINTS