ID   AAE16_ARATH             Reviewed;         722 AA.
AC   Q9LK39; Q8LRT1;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Probable acyl-activating enzyme 16, chloroplastic;
DE            EC=6.2.1.-;
DE   Flags: Precursor;
GN   Name=AAE16; OrderedLocusNames=At3g23790; ORFNames=MYM9.14;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(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   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).
RN   [5]
RP   FUNCTION.
RX   PubMed=16262711; DOI=10.1111/j.1365-313x.2005.02553.x;
RA   Koo A.J., Fulda M., Browse J., Ohlrogge J.B.;
RT   "Identification of a plastid acyl-acyl carrier protein synthetase in
RT   Arabidopsis and its role in the activation and elongation of exogenous
RT   fatty acids.";
RL   Plant J. 44:620-632(2005).
CC   -!- FUNCTION: May be involved in the activation of fatty acids to acyl-
CC       carrier-protein. {ECO:0000250, ECO:0000269|PubMed:16262711}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AF503771; AAM28629.1; -; mRNA.
DR   EMBL; AP000377; BAB01855.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76814.1; -; Genomic_DNA.
DR   RefSeq; NP_189021.2; NM_113283.4.
DR   AlphaFoldDB; Q9LK39; -.
DR   SMR; Q9LK39; -.
DR   STRING; 3702.AT3G23790.1; -.
DR   PaxDb; Q9LK39; -.
DR   PRIDE; Q9LK39; -.
DR   ProteomicsDB; 244519; -.
DR   EnsemblPlants; AT3G23790.1; AT3G23790.1; AT3G23790.
DR   GeneID; 821961; -.
DR   Gramene; AT3G23790.1; AT3G23790.1; AT3G23790.
DR   KEGG; ath:AT3G23790; -.
DR   Araport; AT3G23790; -.
DR   TAIR; locus:2095173; AT3G23790.
DR   eggNOG; KOG1256; Eukaryota.
DR   HOGENOM; CLU_000022_45_5_1; -.
DR   InParanoid; Q9LK39; -.
DR   OMA; GWIAPHC; -.
DR   OrthoDB; 806831at2759; -.
DR   PhylomeDB; Q9LK39; -.
DR   BioCyc; ARA:AT3G23790-MON; -.
DR   PRO; PR:Q9LK39; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LK39; baseline and differential.
DR   Genevisible; Q9LK39; AT.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IGI:TAIR.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 2.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020459; AMP-binding.
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   PRINTS; PR00154; AMPBINDING.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Fatty acid metabolism; Ligase; Lipid metabolism; Plastid;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..47
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           48..722
FT                   /note="Probable acyl-activating enzyme 16, chloroplastic"
FT                   /id="PRO_0000415726"
FT   CONFLICT        16
FT                   /note="S -> C (in Ref. 1; AAM28629)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   722 AA;  81148 MW;  87F9FBCADFDBCE8F CRC64;
     MASTSLGASI LVSHCSSAPE FQVSGMRLVF GYKAFGCRTS RRGFRVRCES KIQEKELRRC
     SPFLERLSLP REAALSSNEW KSVPDIWRSS VEKYGDRVAV VDPYHDPPST FTYRQLEQEI
     LDFVEGLRVV GVKADEKIAL FADNSCRWLV ADQGIMATGA VNVVRGSRSS VEELLQIYCH
     SESVALVVDN PEFFNRIAES FSYKAAPKFV ILLWGEKSSL VTAGRHTPVY SYNEIKKFGQ
     ERRAKFARSN DSGKYEYEYI DPDDIATIMY TSGTTGNPKG VMLTHQNLLH QIRNLSDFVP
     AEAGERFLSM LPSWHAYERA CEYFIFTCGV EQKYTSIRFL KDDLKRYQPH YLISVPLVYE
     TLYSGIQKQI SASSPARKFL ALTLIKVSLA YTEMKRVYEG LCLTKNQKPP MYIVSLVDWL
     WARVVAFFLW PLHMLAEKLV HRKIRSSIGI TKAGVSGGGS LPMHVDKFFE AIGVNVQNGY
     GLTETSPVVS ARRLRCNVLG SVGHPIKDTE FKIVDHETGT VLPPGSKGIV KVRGPPVMKG
     YYKNPLATKQ VIDDDGWFNT GDMGWITPQH STGRSRSCGG VIVLEGRAKD TIVLSTGENV
     EPLEIEEAAM RSNLIQQIVV IGQDQRRLGA IVIPNKEAAE GAAKQKISPV DSEVNELSKE
     TITSMVYEEL RKWTSQCSFQ VGPVLIVDEP FTIDNGLMTP TMKIRRDKVV DQYKNEIERL
     YK