AEE10_ARATH
ID AEE10_ARATH Reviewed; 549 AA.
AC Q9LPK7; A0ME81; Q8LRT3;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Probable acyl-activating enzyme 10;
DE EC=6.2.1.-;
DE AltName: Full=AMP-binding protein 10;
DE Short=AtAMPBP10;
GN Name=AEE10; Synonyms=AMPBP10; OrderedLocusNames=At1g21530;
GN ORFNames=F24J8.13;
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] (ISOFORM 2).
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=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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LPK7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LPK7-2; Sequence=VSP_042324;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots.
CC {ECO:0000269|PubMed:12805634}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28406.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF503769; AAM28627.1; -; mRNA.
DR EMBL; AC015447; AAF87901.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30113.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30114.1; -; Genomic_DNA.
DR EMBL; DQ446270; ABE65638.1; -; mRNA.
DR EMBL; DQ652849; ABK28406.1; ALT_SEQ; mRNA.
DR PIR; B86348; B86348.
DR RefSeq; NP_001077573.1; NM_001084104.2. [Q9LPK7-1]
DR RefSeq; NP_173572.2; NM_102002.2. [Q9LPK7-2]
DR AlphaFoldDB; Q9LPK7; -.
DR SMR; Q9LPK7; -.
DR STRING; 3702.AT1G21530.2; -.
DR PaxDb; Q9LPK7; -.
DR PRIDE; Q9LPK7; -.
DR ProteomicsDB; 244818; -. [Q9LPK7-1]
DR EnsemblPlants; AT1G21530.1; AT1G21530.1; AT1G21530. [Q9LPK7-2]
DR EnsemblPlants; AT1G21530.2; AT1G21530.2; AT1G21530. [Q9LPK7-1]
DR GeneID; 838754; -.
DR Gramene; AT1G21530.1; AT1G21530.1; AT1G21530. [Q9LPK7-2]
DR Gramene; AT1G21530.2; AT1G21530.2; AT1G21530. [Q9LPK7-1]
DR KEGG; ath:AT1G21530; -.
DR Araport; AT1G21530; -.
DR TAIR; locus:2027012; AT1G21530.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_5_1; -.
DR InParanoid; Q9LPK7; -.
DR OMA; GSAACMR; -.
DR OrthoDB; 312083at2759; -.
DR PhylomeDB; Q9LPK7; -.
DR BioCyc; ARA:AT1G21530-MON; -.
DR PRO; PR:Q9LPK7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPK7; baseline and differential.
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 Alternative splicing; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Reference proteome.
FT CHAIN 1..549
FT /note="Probable acyl-activating enzyme 10"
FT /id="PRO_0000415721"
FT VAR_SEQ 299..300
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12177484"
FT /id="VSP_042324"
FT CONFLICT 387
FT /note="S -> L (in Ref. 4; ABK28406)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 549 AA; 60800 MW; A56F91B0FE1E200B CRC64;
MELLLPHPSN STPLTVLGFL DRAASVYGDC PSILHTANTV HTWSETHNRC LRIASALTSS
SIGIKQGQVV SVVGPNVPSV YELQFAVPMS GAILNNINPR LDAHALSVLL RHSESRLVFV
DHRSISLVLE AVSLFTQHEK PHLVLLDDDQ ENDSSSASDF LDTYEEIMER GNSRFKWIRP
QTEWQPMVLN YTSGTTSSPK GVVLSHRAIF MLTVSSLLDW SVPNRPVYLW TLPMFHANGW
GYTWGTAAVG ATNICTRRVD APTIYNLIDK HNVTHMCAAP MVLNMLINYP LSTPLKNPVQ
VMTSGAPPPA TIISRAESLG FNVSHSYGLT ETSGPVVSCA WKPKWDHLDP LERARLKSRQ
GVRTLGFTEV DVRDRKTGKS VKHDGVSVGE IVFRGSSVML GYYKDPQGTA ACMREDGWFY
SGDIGVIHKD GYLEIKDRSK DVIICGGENI SSAEIETVLY TNPVVKEAAV VAKPDKMWGE
TPCAFVSLKC DNNGDGSVPV TEREIREFCK TKLPKYMVPR KVIFQEELPK TSTGKIQKFL
LRQMAKTLS
