FAHD2_ARATH
ID FAHD2_ARATH Reviewed; 224 AA.
AC Q9LUR3;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Probable acylpyruvase FAHD2, mitochondrial {ECO:0000305};
DE EC=3.7.1.5 {ECO:0000305};
DE AltName: Full=Fumarylacetoacetate hydrolase domain-containing protein 2 {ECO:0000305};
DE Short=FAH domain-containing protein 2 {ECO:0000305};
DE Flags: Precursor;
GN Name=FAHD2 {ECO:0000305};
GN OrderedLocusNames=At3g16700 {ECO:0000312|Araport:AT3G16700};
GN ORFNames=MGL6.17 {ECO:0000312|EMBL:BAB02762.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=20018591; DOI=10.1104/pp.109.147942;
RA Tan Y.-F., O'Toole N., Taylor N.L., Millar A.H.;
RT "Divalent metal ions in plant mitochondria and their role in interactions
RT with proteins and oxidative stress-induced damage to respiratory
RT function.";
RL Plant Physiol. 152:747-761(2010).
CC -!- FUNCTION: Probable acylpyruvase. Binds copper in vitro.
CC {ECO:0000269|PubMed:20018591}.
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:0000305};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20018591}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of EST are produced. According to EST sequences.
CC {ECO:0000305};
CC Name=1;
CC IsoId=Q9LUR3-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
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DR EMBL; AB022217; BAB02762.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75853.1; -; Genomic_DNA.
DR EMBL; AY087490; AAM65033.1; -; mRNA.
DR RefSeq; NP_188292.1; NM_112543.3. [Q9LUR3-1]
DR AlphaFoldDB; Q9LUR3; -.
DR SMR; Q9LUR3; -.
DR STRING; 3702.AT3G16700.1; -.
DR PaxDb; Q9LUR3; -.
DR PRIDE; Q9LUR3; -.
DR ProteomicsDB; 222345; -. [Q9LUR3-1]
DR EnsemblPlants; AT3G16700.1; AT3G16700.1; AT3G16700. [Q9LUR3-1]
DR GeneID; 820922; -.
DR Gramene; AT3G16700.1; AT3G16700.1; AT3G16700. [Q9LUR3-1]
DR KEGG; ath:AT3G16700; -.
DR Araport; AT3G16700; -.
DR TAIR; locus:2089373; AT3G16700.
DR eggNOG; KOG1535; Eukaryota.
DR HOGENOM; CLU_028458_5_0_1; -.
DR InParanoid; Q9LUR3; -.
DR OMA; PPRTENY; -.
DR PhylomeDB; Q9LUR3; -.
DR BioCyc; ARA:AT3G16700-MON; -.
DR PRO; PR:Q9LUR3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUR3; baseline and differential.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0018773; F:acetylpyruvate hydrolase activity; IBA:GO_Central.
DR GO; GO:0047621; F:acylpyruvate hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
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 Alternative splicing; Hydrolase; Metal-binding; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 31..224
FT /note="Probable acylpyruvase FAHD2, mitochondrial"
FT /id="PRO_0000442051"
FT BINDING 67
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q6P587"
FT BINDING 69
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q6P587"
FT BINDING 98
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q6P587"
SQ SEQUENCE 224 AA; 24417 MW; F4518841E87F9571 CRC64;
MATSMIQRLF KQGTKIVGVG LNYASHAKEL GNALPKDPIV FLKPTSSYLE NGGTIEIPHP
LDSLHHEVEL AVVIGQKARD VPERLAMNYI GGYALALDMT ARELQVSAMA SGLPCTLAKG
QDTFTPISSV LPKAMVLDPN NLELWLKVDD ETRQKGWTKD MIFKVPYLIS YISSVMTLFK
GDVILTGTPE GIGPVKIGQK ITAGITGLSE VQFDVGRRLK PLLR
