AAE6_ARATH
ID AAE6_ARATH Reviewed; 550 AA.
AC Q9FFE9; Q8RY75;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Probable acyl-activating enzyme 6;
DE EC=6.2.1.-;
DE AltName: Full=AMP-binding protein 6;
DE Short=AtAMPBP6;
GN Name=AAE6; Synonyms=AMPBP6; OrderedLocusNames=At5g16340; ORFNames=MQK4.6;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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] OF 2-550.
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 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).
CC -!- FUNCTION: May act as an acid--thiol ligase that activates carboxylic
CC acids by forming acyl-CoAs. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots, leaves, stems 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; AF503765; AAM28623.1; -; mRNA.
DR EMBL; AB005242; BAB09601.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92281.1; -; Genomic_DNA.
DR EMBL; AY074543; AAL69511.1; -; mRNA.
DR RefSeq; NP_197138.1; NM_121639.3.
DR AlphaFoldDB; Q9FFE9; -.
DR SMR; Q9FFE9; -.
DR STRING; 3702.AT5G16340.1; -.
DR iPTMnet; Q9FFE9; -.
DR PaxDb; Q9FFE9; -.
DR PRIDE; Q9FFE9; -.
DR ProMEX; Q9FFE9; -.
DR ProteomicsDB; 245108; -.
DR EnsemblPlants; AT5G16340.1; AT5G16340.1; AT5G16340.
DR GeneID; 831495; -.
DR Gramene; AT5G16340.1; AT5G16340.1; AT5G16340.
DR KEGG; ath:AT5G16340; -.
DR Araport; AT5G16340; -.
DR TAIR; locus:2171357; AT5G16340.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_5_1; -.
DR InParanoid; Q9FFE9; -.
DR OMA; IQIRGPW; -.
DR OrthoDB; 312083at2759; -.
DR PhylomeDB; Q9FFE9; -.
DR BioCyc; ARA:AT5G16340-MON; -.
DR PRO; PR:Q9FFE9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFE9; baseline and differential.
DR Genevisible; Q9FFE9; 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 2: Evidence at transcript level;
KW Fatty acid metabolism; Ligase; Lipid metabolism; Reference proteome.
FT CHAIN 1..550
FT /note="Probable acyl-activating enzyme 6"
FT /id="PRO_0000415717"
SQ SEQUENCE 550 AA; 60132 MW; 619606489AA48F85 CRC64;
MEEMKPCAAN SPPLTPIGFL ERAATVYGDC TSIVYGSNTV YTWRETNLRC LRVASSLSSI
GIGRSDVVSV LSPNTPAMYE LQFAVPMSGA ILNNINTRLD ARTVSVLLRH CESKLLFVDV
FSVDLAVEAV SMMTTDPPIL VVIADKEEEG GVADVADLSK FSYTYDDLIE RGDPGFKWIR
PESEWDPVVL NYTSGTTSAP KGVVHCHRGI FVMSVDSLID WAVPKNPVYL WTLPIFHSNG
WTNPWGIAAV GGTNVCLRKF DAPLIYRLIR DHGVTHMCGA PVVLNMLSAT QESQPLNHPV
NILTAGSPPP ATVLLRAESI GFVISHGYGL TETAGVIVSC AWKPKWNHLP ASDRARLKAR
QGVRTVGFTE IDVVDPESGL SVERNGETVG EIVMRGSSVM LGYLKDPVGT EKALKNGWFY
TGDVGVIHSD GYLEIKDRSK DIIITGGENV SSVEVETVLY TIPAVNEVAV VARPDEFWGE
TPCAFVSLKN GFSGKPTEEE LMEYCRKKMP KYMVPKTVSF MDELPKSSTG KVTKFVLRDI
AKKMGDKTIS
