ID   AAE12_ARATH             Reviewed;         578 AA.
AC   Q9SS00; Q84P20; Q94A35;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Probable acyl-activating enzyme 12, peroxisomal;
DE            EC=6.2.1.-;
GN   Name=AAE12; OrderedLocusNames=At1g65890; ORFNames=F12P19.6;
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], TISSUE SPECIFICITY, GENE FAMILY, AND
RP   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).
CC   -!- FUNCTION: May act as an acid--thiol ligase that activates carboxylic
CC       acids by forming acyl-CoAs. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in leaves.
CC       {ECO:0000269|PubMed:12805634}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY250840; AAP03023.1; -; mRNA.
DR   EMBL; AC009513; AAF06050.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34437.1; -; Genomic_DNA.
DR   EMBL; AY050412; AAK91428.1; -; mRNA.
DR   EMBL; AY059657; AAL31150.1; -; mRNA.
DR   PIR; B96683; B96683.
DR   RefSeq; NP_176764.1; NM_105261.2.
DR   AlphaFoldDB; Q9SS00; -.
DR   SMR; Q9SS00; -.
DR   STRING; 3702.AT1G65890.1; -.
DR   PaxDb; Q9SS00; -.
DR   PRIDE; Q9SS00; -.
DR   ProteomicsDB; 243268; -.
DR   EnsemblPlants; AT1G65890.1; AT1G65890.1; AT1G65890.
DR   GeneID; 842901; -.
DR   Gramene; AT1G65890.1; AT1G65890.1; AT1G65890.
DR   KEGG; ath:AT1G65890; -.
DR   Araport; AT1G65890; -.
DR   TAIR; locus:2009714; AT1G65890.
DR   eggNOG; KOG1176; Eukaryota.
DR   HOGENOM; CLU_000022_59_5_1; -.
DR   InParanoid; Q9SS00; -.
DR   OMA; HRSFFTL; -.
DR   OrthoDB; 312083at2759; -.
DR   PhylomeDB; Q9SS00; -.
DR   BioCyc; ARA:AT1G65890-MON; -.
DR   PRO; PR:Q9SS00; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SS00; baseline and differential.
DR   Genevisible; Q9SS00; AT.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; 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   2: Evidence at transcript level;
KW   Fatty acid metabolism; Ligase; Lipid metabolism; Peroxisome;
KW   Reference proteome.
FT   CHAIN           1..578
FT                   /note="Probable acyl-activating enzyme 12, peroxisomal"
FT                   /id="PRO_0000415723"
FT   MOTIF           576..578
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        118
FT                   /note="Y -> D (in Ref. 1; AAP03023)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        174
FT                   /note="L -> S (in Ref. 1; AAP03023)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        478
FT                   /note="H -> Y (in Ref. 4; AAK91428/AAL31150)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   578 AA;  64725 MW;  F13BC4757BA2C85E CRC64;
     MDNLALCEAN NVPLTPITFL KRASECYPNR TSIIYGKTRF TWPQTYDRCC RLAASLISLN
     IGKNDVVSVV APNTPAMYEM HFAVPMAGAV LNPINTRLDA TSIAAILRHA KPKILFIYRS
     FEPLAREILQ LLSSEDSNLN LPVIFIHEID FPKRVSSEES DYECLIQRGE PTPLLLARMF
     CIQDEHDPIS LNYTSGTTAD PKGVVISHRG AYLSTLSAII GWEMGTCPVY LWTLPMFHCN
     GWTFTWGTAA RGGTSVCMRH VTAPEIYKNI EMHNVTHMCC VPTVFNILLK GNSLDLSHRS
     GPVHVLTGGS PPPAALVKKV QRLGFQVMHA YGLTEATGPV LFCEWQDEWN RLPENQQMEL
     KARQGLSILG LTEVDVRNKE TQESVPRDGK TMGEIVMKGS SIMKGYLKNP KATYEAFKHG
     WLNSGDVGVI HPDGHVEIKD RSKDIIISGG ENISSVEVEN IIYKYPKVLE TAVVAMPHPT
     WGETPCAFVV LEKGETNNED REDKLVTKER DLIEYCRENL PHFMCPRKVV FLDELPKNGN
     GKILKPKLRD IAKGLVAEDE VNVRSKVQRP VEHFTSRL