AAE5_ARATH
ID AAE5_ARATH Reviewed; 552 AA.
AC Q9FFE6;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Probable acyl-activating enzyme 5, peroxisomal;
DE EC=6.2.1.-;
DE AltName: Full=AMP-binding protein 5;
DE Short=AtAMPBP5;
GN Name=AAE5; Synonyms=AMPBP5; OrderedLocusNames=At5g16370; ORFNames=MQK4.9;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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 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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
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 in roots, stems and developing seeds.
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; AF503764; AAM28622.1; -; mRNA.
DR EMBL; AB005242; BAB09604.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92284.1; -; Genomic_DNA.
DR RefSeq; NP_197141.1; NM_121642.3.
DR AlphaFoldDB; Q9FFE6; -.
DR SMR; Q9FFE6; -.
DR STRING; 3702.AT5G16370.1; -.
DR PaxDb; Q9FFE6; -.
DR PRIDE; Q9FFE6; -.
DR ProteomicsDB; 245114; -.
DR EnsemblPlants; AT5G16370.1; AT5G16370.1; AT5G16370.
DR GeneID; 831498; -.
DR Gramene; AT5G16370.1; AT5G16370.1; AT5G16370.
DR KEGG; ath:AT5G16370; -.
DR Araport; AT5G16370; -.
DR TAIR; locus:2171402; AT5G16370.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_5_1; -.
DR InParanoid; Q9FFE6; -.
DR OMA; ECTAPCA; -.
DR OrthoDB; 312083at2759; -.
DR PhylomeDB; Q9FFE6; -.
DR BioCyc; ARA:AT5G16370-MON; -.
DR PRO; PR:Q9FFE6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFE6; baseline and differential.
DR Genevisible; Q9FFE6; AT.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
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 1: Evidence at protein level;
KW Fatty acid metabolism; Ligase; Lipid metabolism; Peroxisome;
KW Reference proteome.
FT CHAIN 1..552
FT /note="Probable acyl-activating enzyme 5, peroxisomal"
FT /id="PRO_0000415716"
FT MOTIF 550..552
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 552 AA; 60770 MW; E9B04679AB01590D CRC64;
MEQMKPCAAN SPPLTPIGFL ERAATVYGDC TSIVYGSNTV YTWRETNLRC LRVASSLSSI
GIGRSDVVSV LSPNTPAMYE LQFAVPMSGA ILNNINTRLD ARTVSVLLRH CGSKLLFVDV
FSVDLAVEAI SMMTTDPPIL VFIADKEEEG GDADVADRTK FSYTYDDLIH RGDLDFKWIR
PESEWDPVVL NYTSGTTSAP KGVVHCHRGI FVMSIDSLID WTVPKNPVYL WTLPIFHANG
WSYPWGIAAV GGTNVCLRKF DAPLIYRLIR DHGVTHMCGA PVVLNMLSAT NEFQPLNRPV
NILTAGAPPP AAVLLRAESI GFVISHGYGL TETAGLNVSC AWKPQWNRLP ASDRARLKAR
QGVRTVGFTE IDVVDPESGR SVERNGETVG EIVMRGSSIM LGYLKDPVGT EKALKNGWFY
TGDVGVIHSD GYLEIKDRSK DIIITGGENV SSVEVETVLY TNPAVNEVAV VARPDVFWGE
TPCAFVSLKS GLTQRPTEVE MIEYCRKKMP KYMVPKTVSF VDELPKTSTG KVMKFVLREI
AKKMGTTRLS RM
