AEE7_ARATH
ID AEE7_ARATH Reviewed; 569 AA.
AC Q8VZF1; Q9LSQ0;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Acetate/butyrate--CoA ligase AAE7, peroxisomal;
DE EC=6.2.1.1;
DE EC=6.2.1.2;
DE AltName: Full=AMP-binding protein 7;
DE Short=AtAMPBP7;
DE AltName: Full=Acetyl-CoA synthetase;
DE AltName: Full=Acyl-activating enzyme 7;
DE AltName: Full=Butyryl-CoA synthetase;
DE AltName: Full=Protein ACETATE NON-UTILIZING 1;
GN Name=AAE7; Synonyms=ACN1, AMPBP7; OrderedLocusNames=At3g16910;
GN ORFNames=K14A17.23;
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 [MRNA].
RX PubMed=12177484; DOI=10.1104/pp.003269;
RA Shockey J.M., Fulda M.S., Browse J.A.;
RT "Arabidopsis contains nine long-chain acyl-coenzyme A synthetase genes that
RT participate in fatty acid and glycerolipid metabolism.";
RL Plant Physiol. 129:1710-1722(2002).
RN [2]
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 [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 FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, GENE FAMILY, AND
RP NOMENCLATURE.
RX PubMed=12805634; DOI=10.1104/pp.103.020552;
RA Shockey J.M., Fulda M.S., Browse J.;
RT "Arabidopsis contains a large superfamily of acyl-activating enzymes.
RT Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme
RT a synthetases.";
RL Plant Physiol. 132:1065-1076(2003).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=14963767; DOI=10.1007/s00438-004-0985-9;
RA Hooks M.A., Turner J.E., Murphy E.C., Graham I.A.;
RT "Acetate non-utilizing mutants of Arabidopsis: evidence that organic acids
RT influence carbohydrate perception in germinating seedlings.";
RL Mol. Genet. Genomics 271:249-256(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15533942; DOI=10.1074/jbc.m407291200;
RA Turner J.E., Greville K., Murphy E.C., Hooks M.A.;
RT "Characterization of Arabidopsis fluoroacetate-resistant mutants reveals
RT the principal mechanism of acetate activation for entry into the glyoxylate
RT cycle.";
RL J. Biol. Chem. 280:2780-2787(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [9]
RP FUNCTION.
RX PubMed=20863290; DOI=10.1042/bst0381230;
RA Hooks M.A., Allen E., Wattis J.A.;
RT "Modelling the peroxisomal carbon leak during lipid mobilization in
RT Arabidopsis.";
RL Biochem. Soc. Trans. 38:1230-1233(2010).
RN [10]
RP FUNCTION.
RX PubMed=21557725; DOI=10.1042/bj20101764;
RA Allen E., Moing A., Wattis J.A., Larson T., Maucourt M., Graham I.A.,
RA Rolin D., Hooks M.A.;
RT "Evidence that ACN1 (acetate non-utilizing 1) prevents carbon leakage from
RT peroxisomes during lipid mobilization in Arabidopsis seedlings.";
RL Biochem. J. 437:505-513(2011).
CC -!- FUNCTION: Peroxisomal acetate/butyrate--CoA ligase that is probably
CC involved in the activation of exogenous acetate for entry into the
CC glyoxylate cycle. May play a role to prevent carbon loss from
CC peroxisomes during lipid mobilization. In vitro, is active with both
CC acetate and butyrate. {ECO:0000269|PubMed:12805634,
CC ECO:0000269|PubMed:15533942, ECO:0000269|PubMed:20863290,
CC ECO:0000269|PubMed:21557725}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:456215; EC=6.2.1.1;
CC Evidence={ECO:0000269|PubMed:12805634};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty
CC acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2;
CC Evidence={ECO:0000269|PubMed:12805634};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:15533942}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC developing seeds. {ECO:0000269|PubMed:12805634,
CC ECO:0000269|PubMed:15533942}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but seedlings have a strong decrease in glutamine and are
CC resistant to the toxic acetate analog monofluoroacetic acid.
CC {ECO:0000269|PubMed:14963767, ECO:0000269|PubMed:15533942}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA94975.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF503766; AAM28624.1; -; mRNA.
DR EMBL; AB026636; BAA94975.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75883.1; -; Genomic_DNA.
DR EMBL; AY065002; AAL57649.1; -; mRNA.
DR EMBL; AY090269; AAL90930.1; -; mRNA.
DR RefSeq; NP_188316.1; NM_112567.4.
DR AlphaFoldDB; Q8VZF1; -.
DR SMR; Q8VZF1; -.
DR STRING; 3702.AT3G16910.1; -.
DR PaxDb; Q8VZF1; -.
DR PRIDE; Q8VZF1; -.
DR ProteomicsDB; 244766; -.
DR EnsemblPlants; AT3G16910.1; AT3G16910.1; AT3G16910.
DR GeneID; 820946; -.
DR Gramene; AT3G16910.1; AT3G16910.1; AT3G16910.
DR KEGG; ath:AT3G16910; -.
DR Araport; AT3G16910; -.
DR TAIR; locus:2086122; AT3G16910.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_5_1; -.
DR InParanoid; Q8VZF1; -.
DR OMA; FPWSVTA; -.
DR OrthoDB; 312083at2759; -.
DR PhylomeDB; Q8VZF1; -.
DR BioCyc; ARA:AT3G16910-MON; -.
DR PRO; PR:Q8VZF1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8VZF1; baseline and differential.
DR Genevisible; Q8VZF1; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0047760; F:butyrate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006083; P:acetate metabolic process; IDA:UniProtKB.
DR GO; GO:0019605; P:butyrate metabolic process; IDA:UniProtKB.
DR GO; GO:0006097; P:glyoxylate cycle; IDA:TAIR.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
PE 1: Evidence at protein level;
KW Fatty acid metabolism; Ligase; Lipid metabolism; Peroxisome;
KW Reference proteome.
FT CHAIN 1..569
FT /note="Acetate/butyrate--CoA ligase AAE7, peroxisomal"
FT /id="PRO_0000415718"
FT MOTIF 567..569
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 569 AA; 62956 MW; 43AF315EB3C15CBB CRC64;
MAATKWRDID DLPKIPANYT ALTPLWFLDR AAVVHPTRKS VIHGSREYTW RQTYDRCRRL
ASALADRSIG PGSTVAIIAP NIPAMYEAHF GVPMCGAVLN CVNIRLNAPT VAFLLSHSQS
SVIMVDQEFF TLAEDSLRLM EEKAGSSFKR PLLIVIGDHT CAPESLNRAL SKGAIEYEDF
LATGDPNYPW QPPADEWQSI ALGYTSGTTA SPKGVVLHHR GAYIMALSNP LIWGMQDGAV
YLWTLPMFHC NGWCFPWSLA VLSGTSICLR QVTAKEVYSM IAKYKVTHFC AAPVVLNAIV
NAPKEDTILP LPHTVHVMTA GAAPPPSVLF SMNQKGFRVA HTYGLSETYG PSTVCAWKPE
WDSLPPETQA KLNARQGVRY TGMEQLDVID TQTGKPVPAD GKTAGEIVFR GNMVMKGYLK
NPEANKETFA GGWFHSGDIA VKHPDNYIEI KDRSKDVIIS GGENISSVEV ENVVYHHPAV
LEASVVARPD ERWQESPCAF VTLKSDYEKH DQNKLAQDIM KFCREKLPAY WVPKSVVFGP
LPKTATGKIQ KHILRTKAKE MGPVPRSRL
