AAE8_ARATH
ID AAE8_ARATH Reviewed; 544 AA.
AC Q9LQS1; Q8LRT4;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable acyl-activating enzyme 8;
DE EC=6.2.1.-;
DE AltName: Full=AMP-binding protein 8;
DE Short=AtAMPBP8;
GN Name=AAE8; Synonyms=AMPBP8; OrderedLocusNames=At1g75960; ORFNames=T4O12.18;
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=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 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,
CC flowers and 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; AF503767; AAM28625.1; -; mRNA.
DR EMBL; AC007396; AAF26762.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35781.1; -; Genomic_DNA.
DR EMBL; AY070450; AAL49853.1; -; mRNA.
DR EMBL; AY142663; AAN13201.1; -; mRNA.
DR RefSeq; NP_177724.1; NM_106246.4.
DR AlphaFoldDB; Q9LQS1; -.
DR SMR; Q9LQS1; -.
DR STRING; 3702.AT1G75960.1; -.
DR iPTMnet; Q9LQS1; -.
DR PaxDb; Q9LQS1; -.
DR PRIDE; Q9LQS1; -.
DR ProteomicsDB; 244506; -.
DR EnsemblPlants; AT1G75960.1; AT1G75960.1; AT1G75960.
DR GeneID; 843929; -.
DR Gramene; AT1G75960.1; AT1G75960.1; AT1G75960.
DR KEGG; ath:AT1G75960; -.
DR Araport; AT1G75960; -.
DR TAIR; locus:2204360; AT1G75960.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_5_1; -.
DR InParanoid; Q9LQS1; -.
DR OMA; ESNRIAH; -.
DR OrthoDB; 312083at2759; -.
DR PhylomeDB; Q9LQS1; -.
DR BioCyc; ARA:AT1G75960-MON; -.
DR PRO; PR:Q9LQS1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LQS1; baseline and differential.
DR Genevisible; Q9LQS1; 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..544
FT /note="Probable acyl-activating enzyme 8"
FT /id="PRO_0000415719"
FT CONFLICT 3..5
FT /note="DLK -> E (in Ref. 1; AAM28625)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 59711 MW; 8A22CF91AFB3C66B CRC64;
MEDLKPSAAN SLPLTLLGFL ERAATVYGDC TSIVYGNSTV YTWRETNHRC LCVASALSSI
GIGRSDVVSV LSANTPEMYE LQFSVPMSGA ILNNINTRLD ARTVSVLLRH CESKLLFVDF
FYSDLAVEAI TMLLNPPILV LIANEEEEEG GAEVTERSKF CYLYSDLITR GNPDFKWIRP
GSEWDPIVVN YTSGTTSSPK GVVHCHRGIF VMTLDSLTDW AVPKTPVYLW TLPIFHANGW
TYPWGIAAVG GTNVCVRKLH APSIYHLIRD HGVTHMYGAP IVLQILSASQ ESDQPLKSPV
NFLTAGSSPP ATVLLRAESL GFIVSHGYGL TETAGVIVSC AWKPNWNRLP ASDQAQLKSR
QGVRTVGFSE IDVVDPESGR SVERDGETVG EIVLRGSSIM LGYLKNPIGT QNSFKNGWFF
TGDLGVIHGD GYLEIKDRSK DVIISGGENV SSVEVEAVLY TNPAVNEAAV VARPDEFWGE
TPCAFVSLKP GLTRKPTDKE IIEYCKYKMP RYMAPKTVSF LEELPKTSTG KIIKSLLKEI
AKNM
