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FAHD1_ARATH
ID   FAHD1_ARATH             Reviewed;         223 AA.
AC   Q93ZE5; O23443;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Probable acylpyruvase FAHD1, mitochondrial {ECO:0000305};
DE            EC=3.7.1.5 {ECO:0000305};
DE   AltName: Full=Fumarylacetoacetate hydrolase domain-containing protein 1 {ECO:0000305};
DE            Short=FAH domain-containing protein 1 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=FAHD1 {ECO:0000305};
GN   OrderedLocusNames=At4g15940 {ECO:0000312|Araport:AT4G15940};
GN   ORFNames=dl4011w {ECO:0000312|EMBL:CAB46032.1},
GN   FCAALL.203 {ECO:0000312|EMBL:CAB78636.1};
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=9461215; DOI=10.1038/35140;
RA   Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA   Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA   Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA   Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA   De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA   Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA   Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA   Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA   Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA   Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA   Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA   Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT   "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT   thaliana.";
RL   Nature 391:485-488(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, 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   -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AEE83668.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB46032.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB78636.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; Z97340; CAB46032.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161542; CAB78636.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE83668.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY057593; AAL14388.1; -; mRNA.
DR   EMBL; BT020563; AAW70409.1; -; mRNA.
DR   EMBL; AY088072; AAM65618.1; -; mRNA.
DR   PIR; F85176; F85176.
DR   RefSeq; NP_193329.1; NM_117686.5.
DR   AlphaFoldDB; Q93ZE5; -.
DR   SMR; Q93ZE5; -.
DR   STRING; 3702.AT4G15940.1; -.
DR   PeptideAtlas; Q93ZE5; -.
DR   PRIDE; Q93ZE5; -.
DR   ProteomicsDB; 230956; -.
DR   GeneID; 827276; -.
DR   KEGG; ath:AT4G15940; -.
DR   Araport; AT4G15940; -.
DR   TAIR; locus:2129815; AT4G15940.
DR   eggNOG; KOG1535; Eukaryota.
DR   OrthoDB; 1216556at2759; -.
DR   PRO; PR:Q93ZE5; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q93ZE5; 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; IDA: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   Hydrolase; Metal-binding; Mitochondrion; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..30
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..223
FT                   /note="Probable acylpyruvase FAHD1, mitochondrial"
FT                   /id="PRO_0000442050"
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"
FT   CONFLICT        180
FT                   /note="Missing (in Ref. 2; CAB46032/CAB78636/AEE83668)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   223 AA;  24283 MW;  F2E0717062868B3C CRC64;
     MATSMIQRMF KQGTKIVCVG RNYAAHAKEL GNAVPKEPVI FLKPTSSYLE NGGTIEIPHP
     LDSLHHEVEL ALVIGQKARD VPESIAMDYI GGYAVALDMT ARELQASAKA SGLPWTVAKG
     QDTFTPISSV LPKAMVRDPD NLELWLKVDG ETRQKGLTKD MIFKVPYLIS YISSIMTLYE
     GDVILTGTPE GVGPVKIGQK ITAGITGLSE VQFDVERRVK PLS
 
 
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