AAE2_ARATH
ID AAE2_ARATH Reviewed; 603 AA.
AC Q9SEY5;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Isovalerate--CoA ligase AAE2 {ECO:0000303|PubMed:23300257};
DE EC=6.2.1.- {ECO:0000269|PubMed:23300257};
DE AltName: Full=3-methylpentanoate--CoA ligase AAE2 {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 2 {ECO:0000303|PubMed:12177484};
DE Short=AtAMPBP2 {ECO:0000303|PubMed:12177484};
DE AltName: Full=Acyl-activating enzyme 2 {ECO:0000303|PubMed:12805634};
DE AltName: Full=Butanoate--CoA ligase AAE2 {ECO:0000305|PubMed:23300257};
DE EC=6.2.1.- {ECO:0000269|PubMed:23300257};
DE AltName: Full=Hexanoate--CoA ligase AAE2 {ECO:0000305|PubMed:23300257};
DE EC=6.2.1.- {ECO:0000269|PubMed:23300257};
DE AltName: Full=Pentanoate--CoA ligase AAE2 {ECO:0000305|PubMed:23300257};
DE EC=6.2.1.- {ECO:0000269|PubMed:23300257};
GN Name=AAE2 {ECO:0000303|PubMed:12805634};
GN Synonyms=AMPBP2 {ECO:0000303|PubMed:12177484};
GN OrderedLocusNames=At2g17650 {ECO:0000312|Araport:AT2G17650};
GN ORFNames=T17A5.12 {ECO:0000312|EMBL:AAM15484.1};
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 [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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
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 [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 isovalerate to produce 3-
CC methylbutanoyl-CoA (PubMed:23300257). Can also use butanoate,
CC pentanoate, hexanoate, 3-methylpentanoate and 4-methylpentanoate as
CC substrates with a lower efficiency (PubMed:23300257).
CC {ECO:0000269|PubMed:23300257}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + isovalerate = 3-methylbutanoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:46184, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:48942, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57345, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46185;
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 + 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 + 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=3-methylpentanoate + ATP + CoA = 3-methylpentanoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:66992, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:167610,
CC ChEBI:CHEBI:167613, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:23300257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66993;
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 -!- TISSUE SPECIFICITY: Expressed at low levels in leaves, flowers and
CC developing seeds. {ECO:0000269|PubMed:12805634}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AF503761; AAM28619.1; -; mRNA.
DR EMBL; AC007509; AAM15484.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06661.1; -; Genomic_DNA.
DR EMBL; AK118689; BAC43283.1; -; mRNA.
DR EMBL; BT005926; AAO64861.1; -; mRNA.
DR PIR; G84554; G84554.
DR PIR; T08866; T08866.
DR RefSeq; NP_179356.1; NM_127319.4.
DR AlphaFoldDB; Q9SEY5; -.
DR SMR; Q9SEY5; -.
DR STRING; 3702.AT2G17650.1; -.
DR iPTMnet; Q9SEY5; -.
DR PaxDb; Q9SEY5; -.
DR PRIDE; Q9SEY5; -.
DR ProteomicsDB; 244389; -.
DR EnsemblPlants; AT2G17650.1; AT2G17650.1; AT2G17650.
DR GeneID; 816272; -.
DR Gramene; AT2G17650.1; AT2G17650.1; AT2G17650.
DR KEGG; ath:AT2G17650; -.
DR Araport; AT2G17650; -.
DR TAIR; locus:2057249; AT2G17650.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_5_1; -.
DR InParanoid; Q9SEY5; -.
DR OMA; YGPGTFC; -.
DR OrthoDB; 312083at2759; -.
DR PhylomeDB; Q9SEY5; -.
DR BioCyc; ARA:AT2G17650-MON; -.
DR PRO; PR:Q9SEY5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SEY5; baseline and differential.
DR Genevisible; Q9SEY5; AT.
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 Fatty acid metabolism; Ligase; Lipid metabolism; Reference proteome.
FT CHAIN 1..603
FT /note="Isovalerate--CoA ligase AAE2"
FT /id="PRO_0000415714"
SQ SEQUENCE 603 AA; 67462 MW; DFF58A4972C9F57F CRC64;
MRFLLTKRAF RIFNPRFQRL WLTSSPFSST SNSGGFPDDS EPESWRTIEG LLRSPANFSP
LSPITFLERS AKVYRDRTSL VFGSVKHTWF QTYQRCLRLA SALTNLGISR GDVVAALAPN
VPAMHELHFA VPMAGLILCP LNTRLDPSTL SVLLAHSEAK ILFVDHQLLE IAHGALDLLA
KSDKTRKSLK LVLISQSNDD DDSDEDSSST FASKYSFDYE YETLLKSGDS EFEIIKPRCE
WDPISINYTS GTTSRPKGVV YSHRGAYLNS LATVFLHQMS VYPVYLWTVP MFHCNGWCLV
WGVAAQGGTN ICLRKVSPKM IFKNIAMHKV THMGGAPTVL NMIVNYTVTE HKPLPHRVEI
MTGGSPPLPQ ILAKMEELGF NVSHLYGLTE TYGPGTHCVW KPEWDSLSLE ERTKLKARQG
VQHLGLEGLD VKDPLTMETV PDDGLTMGEV MFRGNTVMSG YFKDIEATRK AFEGDWFHSG
DLAVKYPDGY IEIKDRLKDV IISGGENISS VEVERVLCSH QAVLEAAVVA RPDHHWGQTP
CGFVKLKEGF DTIKPEEIIG FCRDHLPHYM APKTIVFGDI PKTSTGKVQK YLLRKKADEM
GSL
