AAE1_ARATH
ID AAE1_ARATH Reviewed; 556 AA.
AC F4HUK6; Q8LRT6; Q94JT9; Q9LM95; Q9LMW3;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Butanoate--CoA ligase AAE1 {ECO:0000305|PubMed:23300257};
DE EC=6.2.1.- {ECO:0000269|PubMed:23300257};
DE AltName: Full=4-methylpentanoate--CoA ligase AAE2 {ECO:0000305|PubMed:23300257};
DE EC=6.2.1.- {ECO:0000269|PubMed:23300257};
DE AltName: Full=AMP-binding protein 1 {ECO:0000303|PubMed:12177484};
DE Short=AtAMPBP1 {ECO:0000303|PubMed:12177484};
DE AltName: Full=Acyl-activating enzyme 1, peroxisomal {ECO:0000303|PubMed:12805634};
DE AltName: Full=Hexanoate--CoA ligase CCL3 {ECO:0000305|PubMed:23300257};
DE EC=6.2.1.- {ECO:0000269|PubMed:23300257};
DE AltName: Full=Pentanoate--CoA ligase CCL3 {ECO:0000305|PubMed:23300257};
DE EC=6.2.1.- {ECO:0000269|PubMed:23300257};
GN Name=AAE1 {ECO:0000303|PubMed:12805634};
GN Synonyms=AMPBP1 {ECO:0000303|PubMed:12177484};
GN OrderedLocusNames=At1g20560 {ECO:0000312|Araport:AT1G20560};
GN ORFNames=F5M15.12 {ECO:0000312|EMBL:AAF79607.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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].
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-556.
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 [5]
RP TISSUE SPECIFICITY, GENE FAMILY, AND 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 SUBCELLULAR LOCATION.
RX PubMed=19329564; DOI=10.1104/pp.109.137703;
RA Reumann S., Quan S., Aung K., Yang P., Manandhar-Shrestha K., Holbrook D.,
RA Linka N., Switzenberg R., Wilkerson C.G., Weber A.P., Olsen L.J., Hu J.;
RT "In-depth proteome analysis of Arabidopsis leaf peroxisomes combined with
RT in vivo subcellular targeting verification indicates novel metabolic and
RT regulatory functions of peroxisomes.";
RL Plant Physiol. 150:125-143(2009).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23300257; DOI=10.1093/mp/sst004;
RA Xu H., Zhang F., Liu B., Huhman D.V., Sumner L.W., Dixon R.A., Wang G.;
RT "Characterization of the formation of branched short-chain fatty acid:CoAs
RT for bitter acid biosynthesis in hop glandular trichomes.";
RL Mol. Plant 6:1301-1317(2013).
CC -!- FUNCTION: Catalyzes the ligation of CoA on butanoate to produce
CC butanoyl-CoA (PubMed:23300257). Can also use hexanoate, pentanoate and
CC 4-methylpentanoate as substrates with a lower efficiency
CC (PubMed:23300257). {ECO:0000269|PubMed:23300257}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + butanoate + CoA = AMP + butanoyl-CoA + diphosphate;
CC Xref=Rhea:RHEA:46172, ChEBI:CHEBI:17968, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46173;
CC Evidence={ECO:0000269|PubMed:23300257};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexanoate = AMP + diphosphate + hexanoyl-CoA;
CC Xref=Rhea:RHEA:43740, ChEBI:CHEBI:17120, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43741;
CC Evidence={ECO:0000269|PubMed:23300257};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + pentanoate = AMP + diphosphate + pentanoyl-CoA;
CC Xref=Rhea:RHEA:46168, ChEBI:CHEBI:30616, ChEBI:CHEBI:31011,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57389,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46169;
CC Evidence={ECO:0000269|PubMed:23300257};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methylpentanoate + ATP + CoA = 4-methylpentanoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:66988, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:74904,
CC ChEBI:CHEBI:131445, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66989;
CC Evidence={ECO:0000269|PubMed:23300257};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:19329564}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=F4HUK6-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC developing seeds. {ECO:0000269|PubMed:12805634}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79607.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF80642.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC027665; AAF79607.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC069251; AAF80642.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29986.1; -; Genomic_DNA.
DR EMBL; AF372942; AAK50082.1; -; mRNA.
DR EMBL; AY078039; AAL77740.1; -; mRNA.
DR EMBL; AF503760; AAM28618.1; -; mRNA.
DR PIR; G86338; G86338.
DR RefSeq; NP_564116.1; NM_101906.4. [F4HUK6-1]
DR AlphaFoldDB; F4HUK6; -.
DR SMR; F4HUK6; -.
DR STRING; 3702.AT1G20560.1; -.
DR PaxDb; F4HUK6; -.
DR PRIDE; F4HUK6; -.
DR ProteomicsDB; 245090; -. [F4HUK6-1]
DR EnsemblPlants; AT1G20560.1; AT1G20560.1; AT1G20560. [F4HUK6-1]
DR GeneID; 838644; -.
DR Gramene; AT1G20560.1; AT1G20560.1; AT1G20560. [F4HUK6-1]
DR KEGG; ath:AT1G20560; -.
DR Araport; AT1G20560; -.
DR TAIR; locus:2030407; AT1G20560.
DR eggNOG; KOG1176; Eukaryota.
DR InParanoid; F4HUK6; -.
DR OMA; SAMLDNC; -.
DR OrthoDB; 312083at2759; -.
DR PRO; PR:F4HUK6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HUK6; baseline and differential.
DR Genevisible; F4HUK6; AT.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
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; IPR020845; AMP-binding_CS.
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.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Peroxisome; Reference proteome.
FT CHAIN 1..556
FT /note="Butanoate--CoA ligase AAE1"
FT /id="PRO_0000415713"
FT MOTIF 554..556
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT CONFLICT 128
FT /note="E -> D (in Ref. 3; AAK50082/AAL77740)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 556 AA; 61073 MW; 3CE93BF49E4826C1 CRC64;
MKMEGTIKSP ANYVPLTPIS FLDRSAVVYA DRVSIVYGSV KYTWRQTRDR CVRIASALSQ
LGISTGDVVS VLAPNVPAMV ELHFGVPMAG ALLCTLNIRH DSSLVAVLLR HSGTKVIFAD
HQFLQIAEGA CEILSNKGDK VPILVLIPEP LTQSVSRKKR SEEMMEYEDV VAMGKSDFEV
IRPTDECDAI SVNYTSGTTS SPKGVVYSHR GAYLNSLAAV LLNEMHSSPT YLWTNPMFHC
NGWCLLWGVT AIGGTNICLR NVTAKAIFDN ISQHKVTHMG GAPTILNMII NAPESEQKPL
PGKVSFITGA APPPAHVIFK MEELGFSMFH SYGLTETYGP GTICTWKPEW DSLPREEQAK
MKARQGVNHL GLEEIQVKDP VTMRTLPADG VTMGEVVFRG NTVMNGYLKN PEATKEAFKG
GWFWSGDLGV KHPDGYIELK DRSKDIIISG GENISSIEVE STLFTHPCVL EAAVVARPDE
YWGETACAFV KLKDGSKASA EELISYCRDR LPHYMAPRSI VFEDLPKTST GKVQKFVLRT
KAKALVSLSK KGRSKL
