AAE11_ARATH
ID AAE11_ARATH Reviewed; 572 AA.
AC Q9C8D4; Q84P19;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Butyrate--CoA ligase AAE11, peroxisomal;
DE EC=6.2.1.2;
DE AltName: Full=Acyl-activating enzyme 11;
DE AltName: Full=Butyryl-CoA synthetase;
GN Name=AAE11; OrderedLocusNames=At1g66120; ORFNames=F15E12.22;
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], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Wassilewskija;
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 [2]
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 [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 Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Butyrate--CoA ligase that is active in vitro with medium-
CC chain fatty acids, with a preference for hexanoate and octanoate.
CC {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:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers.
CC {ECO:0000269|PubMed:12805634}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AY250841; AAP03024.1; -; mRNA.
DR EMBL; AC026480; AAG51304.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34464.1; -; Genomic_DNA.
DR EMBL; BT004314; AAO42311.1; -; mRNA.
DR EMBL; BT030349; ABO38762.1; -; mRNA.
DR PIR; H96685; H96685.
DR RefSeq; NP_176786.1; NM_105283.3.
DR AlphaFoldDB; Q9C8D4; -.
DR SMR; Q9C8D4; -.
DR BioGRID; 28147; 1.
DR STRING; 3702.AT1G66120.1; -.
DR PaxDb; Q9C8D4; -.
DR PRIDE; Q9C8D4; -.
DR ProteomicsDB; 244558; -.
DR EnsemblPlants; AT1G66120.1; AT1G66120.1; AT1G66120.
DR GeneID; 842926; -.
DR Gramene; AT1G66120.1; AT1G66120.1; AT1G66120.
DR KEGG; ath:AT1G66120; -.
DR Araport; AT1G66120; -.
DR TAIR; locus:2013860; AT1G66120.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_5_1; -.
DR InParanoid; Q9C8D4; -.
DR OMA; YNVPIVQ; -.
DR OrthoDB; 298283at2759; -.
DR PhylomeDB; Q9C8D4; -.
DR BioCyc; ARA:AT1G66120-MON; -.
DR PRO; PR:Q9C8D4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8D4; baseline and differential.
DR Genevisible; Q9C8D4; AT.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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:0019605; P:butyrate metabolic process; IDA:UniProtKB.
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..572
FT /note="Butyrate--CoA ligase AAE11, peroxisomal"
FT /id="PRO_0000415722"
FT MOTIF 570..572
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT CONFLICT 135..139
FT /note="YQSQP -> DQSQA (in Ref. 1; AAP03024)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="Q -> R (in Ref. 1; AAP03024)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="I -> M (in Ref. 1; AAP03024)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="E -> Q (in Ref. 1; AAP03024)"
FT /evidence="ECO:0000305"
FT CONFLICT 495..498
FT /note="EEGL -> DEES (in Ref. 1; AAP03024)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 63941 MW; C9CD11DC6D48D1E6 CRC64;
MDNLVLCEAN NVPLTPITFL KRASECYPNR TSIIYGQTRF TWPQTYDRCC RLAASLLSLN
ITRNDVVSIL APNVPAMYEM HFSVPMTGAV LNPINTRLDA KTIAIILRHA EPKILFVDYE
FAPLIQEVLR LIPTYQSQPH PRIILINEID STTKPFSKEL DYEGLIRKGE PTPSSSASMF
RVHNEHDPIS LNYTSGTTAD PKGVVISHQG AYLSALSSII GWEMGIFPVY LWTLPMFHCN
GWTHTWSVAA RGGTNVCIRH VTAPEIYKNI ELHGVTHMSC VPTVFRFLLE GSRTDQSPKS
SPVQVLTGGS SPPAVLIKKV EQLGFHVMHG YGLTEATGPV LFCEWQDEWN KLPEHQQIEL
QQRQGVRNLT LADVDVKNTK TLESVPRDGK TMGEIVIKGS SLMKGYLKNP KATSEAFKHG
WLNTGDIGVI HPDGYVEIKD RSKDIIISGG ENISSIEVEK VLYMYQEVLE AAVVAMPHPL
WGETPCAFVV LKKGEEGLVT SEGDLIKYCR ENMPHFMCPK KVVFFQELPK NSNGKILKSK
LRDIAKALVV REDDAGSKKV HQRSIEHVSS RL
