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Protein

Acylpyruvase FAHD1, mitochondrial

Gene

Fahd1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable mitochondrial acylpyruvase which is able to hydrolyze acetylpyruvate and fumarylpyruvate in vitro (By similarity). Also has oxaloacetate decarboxylase activity (PubMed:25575590).By similarity1 Publication

Catalytic activityi

A 3-acylpyruvate + H2O = a carboxylate + pyruvate.By similarity
Oxaloacetate = pyruvate + CO2.By similarity

Cofactori

Mg2+By similarity, Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi74 – 741Divalent metal cationBy similarity
Metal bindingi76 – 761Divalent metal cationBy similarity
Metal bindingi105 – 1051Divalent metal cationBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Lyase

Keywords - Ligandi

Calcium, Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Acylpyruvase FAHD1, mitochondrial (EC:3.7.1.5)
Alternative name(s):
Fumarylacetoacetate hydrolase domain-containing protein 1
Oxaloacetate decarboxylaseBy similarity (EC:4.1.1.3By similarity)
Short name:
OAA decarboxylaseBy similarity
Gene namesi
Name:Fahd1
ORF Names:MNCb-4134
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1915886. Fahd1.

Subcellular locationi

  • Mitochondrion By similarity
  • Cytoplasmcytosol By similarity

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: UniProtKB
  • mitochondrial inner membrane Source: MGI
  • mitochondrion Source: MGI
  • nucleoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. Elevated oxaloacetate levels.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030MitochondrionSequence analysisAdd
BLAST
Chaini31 – 227197Acylpyruvase FAHD1, mitochondrialPRO_0000156830Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431PhosphoserineBy similarity
Modified residuei116 – 1161N6-acetyllysineCombined sources
Modified residuei118 – 1181N6-succinyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8R0F8.
MaxQBiQ8R0F8.
PaxDbiQ8R0F8.
PRIDEiQ8R0F8.

PTM databases

iPTMnetiQ8R0F8.
PhosphoSiteiQ8R0F8.

Expressioni

Tissue specificityi

Ubiquitous with higher expression in the liver and the kidney (at protein level).1 Publication

Gene expression databases

CleanExiMM_FAHD1.
GenevisibleiQ8R0F8. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ8R0F8. 4 interactions.
MINTiMINT-1849538.
STRINGi10090.ENSMUSP00000055827.

Structurei

3D structure databases

ProteinModelPortaliQ8R0F8.
SMRiQ8R0F8. Positions 11-227.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FAH family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1535. Eukaryota.
COG0179. LUCA.
GeneTreeiENSGT00530000063832.
HOGENOMiHOG000063753.
HOVERGENiHBG057495.
InParanoidiQ8R0F8.
KOiK01557.
OMAiYVSKIMT.
OrthoDBiEOG7DFXDC.
TreeFamiTF300911.

Family and domain databases

Gene3Di3.90.850.10. 1 hit.
InterProiIPR011234. Fumarylacetoacetase_C-rel.
[Graphical view]
PfamiPF01557. FAA_hydrolase. 1 hit.
[Graphical view]
SUPFAMiSSF56529. SSF56529. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8R0F8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQSCTMAST KPLSRFWEWG KNIVCVGRNY ADHVKEMRST VLSEPVLFLK
60 70 80 90 100
PSTAYAPEGS PVLMPAYCRN LHHEVELGVL LGKRGEAIPE AAAMDYVAGY
110 120 130 140 150
ALCLDMTARD VQEECKKKGL PWTLAKSFTS SCPVSAFVPK EKIPDPHALR
160 170 180 190 200
LWLKVNGELR QEGKTSSMIF SIPYIISYVS KIITLEEGDL ILTGTPKGVG
210 220
PIKENDEIEA GIDGVVSMRF KVKRSEY
Length:227
Mass (Da):25,172
Last modified:October 3, 2012 - v2
Checksum:i62C5AEA14F8F38C5
GO

Sequence cautioni

The sequence BAC32142.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → R in BAC32142 (PubMed:16141072).Curated
Sequence conflicti202 – 2021I → V in BAE34035 (PubMed:16141072).Curated
Sequence conflicti202 – 2021I → V in AAH26949 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB041600 mRNA. Translation: BAA95083.1.
AK044920 mRNA. Translation: BAC32142.1. Different initiation.
AK157292 mRNA. Translation: BAE34035.1.
AK141973 mRNA. Translation: BAE24904.1.
AC166102 Genomic DNA. No translation available.
BC026949 mRNA. Translation: AAH26949.1.
CCDSiCCDS37496.1.
RefSeqiNP_075969.1. NM_023480.2.
UniGeneiMm.347964.

Genome annotation databases

EnsembliENSMUST00000049642; ENSMUSP00000055827; ENSMUSG00000045316.
GeneIDi68636.
KEGGimmu:68636.
UCSCiuc008ayl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB041600 mRNA. Translation: BAA95083.1.
AK044920 mRNA. Translation: BAC32142.1. Different initiation.
AK157292 mRNA. Translation: BAE34035.1.
AK141973 mRNA. Translation: BAE24904.1.
AC166102 Genomic DNA. No translation available.
BC026949 mRNA. Translation: AAH26949.1.
CCDSiCCDS37496.1.
RefSeqiNP_075969.1. NM_023480.2.
UniGeneiMm.347964.

3D structure databases

ProteinModelPortaliQ8R0F8.
SMRiQ8R0F8. Positions 11-227.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8R0F8. 4 interactions.
MINTiMINT-1849538.
STRINGi10090.ENSMUSP00000055827.

PTM databases

iPTMnetiQ8R0F8.
PhosphoSiteiQ8R0F8.

Proteomic databases

EPDiQ8R0F8.
MaxQBiQ8R0F8.
PaxDbiQ8R0F8.
PRIDEiQ8R0F8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000049642; ENSMUSP00000055827; ENSMUSG00000045316.
GeneIDi68636.
KEGGimmu:68636.
UCSCiuc008ayl.1. mouse.

Organism-specific databases

CTDi81889.
MGIiMGI:1915886. Fahd1.

Phylogenomic databases

eggNOGiKOG1535. Eukaryota.
COG0179. LUCA.
GeneTreeiENSGT00530000063832.
HOGENOMiHOG000063753.
HOVERGENiHBG057495.
InParanoidiQ8R0F8.
KOiK01557.
OMAiYVSKIMT.
OrthoDBiEOG7DFXDC.
TreeFamiTF300911.

Miscellaneous databases

NextBioi327606.
PROiQ8R0F8.
SOURCEiSearch...

Gene expression databases

CleanExiMM_FAHD1.
GenevisibleiQ8R0F8. MM.

Family and domain databases

Gene3Di3.90.850.10. 1 hit.
InterProiIPR011234. Fumarylacetoacetase_C-rel.
[Graphical view]
PfamiPF01557. FAA_hydrolase. 1 hit.
[Graphical view]
SUPFAMiSSF56529. SSF56529. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of full-length cDNA clones from mouse brain cDNA library made by oligo-capping method."
    Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Embryo, Spinal ganglion and Spleen.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "Identification of human fumarylacetoacetate hydrolase domain containing protein 1 (FAHD1) as a novel mitochondrial acylpyruvase."
    Pircher H., Straganz G.D., Ehehalt D., Morrow G., Tanguay R.M., Jansen-Durr P.
    J. Biol. Chem. 286:36500-36508(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiFAHD1_MOUSE
AccessioniPrimary (citable) accession number: Q8R0F8
Secondary accession number(s): Q3U020
, Q3UQY4, Q8BLJ7, Q9JJB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: October 3, 2012
Last modified: March 16, 2016
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.