AAE13_ARATH
ID AAE13_ARATH Reviewed; 608 AA.
AC Q8H151; Q8LFU5; Q9LW70;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 2.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Malonate--CoA ligase;
DE EC=6.2.1.n3;
DE AltName: Full=Acyl-activating enzyme 13;
DE AltName: Full=Malonyl-CoA synthetase;
GN Name=AAE13; OrderedLocusNames=At3g16170; ORFNames=MSL1.21;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 25-608.
RC STRAIN=cv. Columbia;
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-608.
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 NUCLEOTIDE SEQUENCE [MRNA] OF 65-608, TISSUE SPECIFICITY, GENE FAMILY, AND
RP 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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21642549; DOI=10.1105/tpc.111.086140;
RA Chen H., Kim H.U., Weng H., Browse J.;
RT "Malonyl-CoA synthetase, encoded by ACYL ACTIVATING ENZYME13, is essential
RT for growth and development of arabidopsis.";
RL Plant Cell 23:2247-2262(2011).
CC -!- FUNCTION: Malonate--CoA ligase that catalyzes the formation of malonyl-
CC CoA directly from malonate and CoA. May be required for the
CC detoxification of malonate. {ECO:0000269|PubMed:21642549}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + malonate = AMP + diphosphate + malonyl-CoA;
CC Xref=Rhea:RHEA:32139, ChEBI:CHEBI:15792, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:456215; EC=6.2.1.n3;
CC Evidence={ECO:0000269|PubMed:21642549};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=530 uM for malonate (at pH 7.5) {ECO:0000269|PubMed:21642549};
CC Vmax=24 umol/min/mg enzyme toward malonate (at pH 7.5)
CC {ECO:0000269|PubMed:21642549};
CC pH dependence:
CC Optimum pH is 6.5-8.0. {ECO:0000269|PubMed:21642549};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21642549}. Nucleus
CC {ECO:0000269|PubMed:21642549}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers. {ECO:0000269|PubMed:12805634,
CC ECO:0000269|PubMed:21642549}.
CC -!- INDUCTION: By abscisic acid (ABA) and osmotic stress.
CC {ECO:0000269|PubMed:21642549}.
CC -!- DISRUPTION PHENOTYPE: Strong defects in growth and development and most
CC of the plants die before flowering. Viable plants have a greatly
CC reduced seed set with a low proportion of viable seed and accumulate
CC malonate and succinate. {ECO:0000269|PubMed:21642549}.
CC -!- MISCELLANEOUS: Plants overexpressing AAE13 show increased sensitivity
CC to exogenous malonate.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM61199.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAN31910.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB02683.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY250842; AAP03025.1; -; mRNA.
DR EMBL; AB012247; BAB02683.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75779.2; -; Genomic_DNA.
DR EMBL; AY084636; AAM61199.1; ALT_INIT; mRNA.
DR EMBL; BT000771; AAN31910.1; ALT_INIT; mRNA.
DR RefSeq; NP_001319565.1; NM_001338210.1.
DR AlphaFoldDB; Q8H151; -.
DR SMR; Q8H151; -.
DR BioGRID; 6196; 2.
DR STRING; 3702.AT3G16170.1; -.
DR PaxDb; Q8H151; -.
DR PRIDE; Q8H151; -.
DR ProteomicsDB; 243269; -.
DR EnsemblPlants; AT3G16170.1; AT3G16170.1; AT3G16170.
DR GeneID; 820862; -.
DR Gramene; AT3G16170.1; AT3G16170.1; AT3G16170.
DR KEGG; ath:AT3G16170; -.
DR Araport; AT3G16170; -.
DR TAIR; locus:2093432; AT3G16170.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_11_1; -.
DR InParanoid; Q8H151; -.
DR OMA; QWAVWAA; -.
DR OrthoDB; 533939at2759; -.
DR PRO; PR:Q8H151; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8H151; baseline and differential.
DR Genevisible; Q8H151; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0090409; F:malonyl-CoA synthetase activity; IDA:TAIR.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IMP:TAIR.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0090410; P:malonate catabolic process; IMP:TAIR.
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 Cytoplasm; Fatty acid metabolism; Ligase; Lipid metabolism; Nucleus;
KW Reference proteome.
FT CHAIN 1..608
FT /note="Malonate--CoA ligase"
FT /id="PRO_0000415724"
FT CONFLICT 38
FT /note="P -> T (in Ref. 4; AAN31910)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="S -> F (in Ref. 3; AAM61199)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="N -> K (in Ref. 3; AAM61199)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 608 AA; 67164 MW; 95A82B449CE1BE62 CRC64;
MTATTTLKSF NYLSLINHRL NHNSYAILSS PLLPRSHPAS TSFSNSGFRF FQSNHLFSSQ
SGSLMEVFKA AFSEASNSCD RIAIKADGKS YSYGQLTSSA LRISKLFLKD DTTNGGQETK
KYEGFGSLKG ARIGIVAKPS AEFVAGVLGT WFSGGVAVPL ALSYPEAELL HVMNDSDISL
LLSTEDHSET MKTIAAKSGA RFHLIPPVVN STSETVACNQ FQDDSFEAEG KFLDDPALIV
YTSGTTGKPK GVVHTHNSIN SQVRMLTEAW EYTSADHFLH CLPLHHVHGL FNALFAPLYA
RSLVEFLPKF SVSGIWRRWR ESYPVNDEKT NDSITVFTGV PTMYTRLIQG YEAMDKEMQD
SSAFAARKLR LMMSGSSALP RPVMHQWESI TGHRLLERYG MTEFVMAMSN PLRGARNAGT
VGKPLPGVEA KIKEDENDAN GVGEICVKSP SLFKEYWNLP EVTKESFTED GYFKTGDAGR
VDEDGYYVIL GRNSADIMKV GGYKLSALEI ESTLLEHPTV AECCVLGLTD NDYGEAVTAI
IIAESAAKKR REDESKPVIT LEELCGWAKD KLAPYKLPTR LLIWESLPRN AMGKVNKKEL
KKSLENQE
