MASY_ARATH
ID MASY_ARATH Reviewed; 562 AA.
AC Q9LZC3;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Malate synthase {ECO:0000303|PubMed:15272001};
DE EC=2.3.3.9 {ECO:0000269|PubMed:15272001};
GN Name=MLS {ECO:0000303|PubMed:15272001};
GN OrderedLocusNames=At5g03860 {ECO:0000312|Araport:AT5G03860};
GN ORFNames=F8F6.70 {ECO:0000312|EMBL:CAB85506.1};
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=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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15272001; DOI=10.1074/jbc.m407380200;
RA Cornah J.E., Germain V., Ward J.L., Beale M.H., Smith S.M.;
RT "Lipid utilization, gluconeogenesis, and seedling growth in Arabidopsis
RT mutants lacking the glyoxylate cycle enzyme malate synthase.";
RL J. Biol. Chem. 279:42916-42923(2004).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=19246395; DOI=10.1073/pnas.0811329106;
RA Lingard M.J., Monroe-Augustus M., Bartel B.;
RT "Peroxisome-associated matrix protein degradation in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:4561-4566(2009).
CC -!- FUNCTION: Does not seem to be essential for lipid utilization and
CC gluconeogenesis in seedlings. {ECO:0000303|PubMed:15272001}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+);
CC Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.3.9;
CC Evidence={ECO:0000269|PubMed:15272001};
CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 2/2. {ECO:0000255|RuleBase:RU000555}.
CC -!- SUBCELLULAR LOCATION: Glyoxysome {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed from 1 to 5 days after seed imbibition
CC (at protein level). {ECO:0000269|PubMed:19246395}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the frequency of mutant seedlings to establish into
CC plantlets with true leaves is decreased under short day conditions.
CC {ECO:0000269|PubMed:15272001}.
CC -!- SIMILARITY: Belongs to the malate synthase family. {ECO:0000305}.
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DR EMBL; AB005235; BAB08612.1; -; Genomic_DNA.
DR EMBL; AL162873; CAB85506.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90663.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90664.1; -; Genomic_DNA.
DR EMBL; AF360126; AAK25836.1; -; mRNA.
DR EMBL; AY051027; AAK93704.1; -; mRNA.
DR PIR; T48413; T48413.
DR RefSeq; NP_001190219.1; NM_001203290.1.
DR RefSeq; NP_196006.1; NM_120467.4.
DR AlphaFoldDB; Q9LZC3; -.
DR SMR; Q9LZC3; -.
DR BioGRID; 16966; 1.
DR STRING; 3702.AT5G03860.1; -.
DR PaxDb; Q9LZC3; -.
DR PRIDE; Q9LZC3; -.
DR ProteomicsDB; 238885; -.
DR EnsemblPlants; AT5G03860.1; AT5G03860.1; AT5G03860.
DR EnsemblPlants; AT5G03860.2; AT5G03860.2; AT5G03860.
DR GeneID; 831690; -.
DR Gramene; AT5G03860.1; AT5G03860.1; AT5G03860.
DR Gramene; AT5G03860.2; AT5G03860.2; AT5G03860.
DR KEGG; ath:AT5G03860; -.
DR Araport; AT5G03860; -.
DR TAIR; locus:2150625; AT5G03860.
DR eggNOG; KOG1261; Eukaryota.
DR HOGENOM; CLU_018928_3_0_1; -.
DR InParanoid; Q9LZC3; -.
DR OMA; CHKRGAP; -.
DR OrthoDB; 358540at2759; -.
DR PhylomeDB; Q9LZC3; -.
DR BioCyc; ARA:AT5G03860-MON; -.
DR BioCyc; MetaCyc:AT5G03860-MON; -.
DR UniPathway; UPA00703; UER00720.
DR PRO; PR:Q9LZC3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZC3; baseline and differential.
DR Genevisible; Q9LZC3; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0004474; F:malate synthase activity; IMP:TAIR.
DR GO; GO:0006097; P:glyoxylate cycle; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd00727; malate_synt_A; 1.
DR Gene3D; 1.20.1220.12; -; 1.
DR Gene3D; 3.20.20.360; -; 1.
DR InterPro; IPR044856; Malate_synth_C_sf.
DR InterPro; IPR011076; Malate_synth_sf.
DR InterPro; IPR006252; Malate_synthA.
DR InterPro; IPR001465; Malate_synthase.
DR InterPro; IPR019830; Malate_synthase_CS.
DR InterPro; IPR046363; MS_N_TIM-barrel_dom.
DR PANTHER; PTHR42902; PTHR42902; 1.
DR Pfam; PF01274; Malate_synthase; 1.
DR PIRSF; PIRSF001363; Malate_synth; 1.
DR SUPFAM; SSF51645; SSF51645; 1.
DR TIGRFAMs; TIGR01344; malate_syn_A; 1.
DR PROSITE; PS00510; MALATE_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Glyoxylate bypass; Glyoxysome; Peroxisome; Reference proteome; Transferase;
KW Tricarboxylic acid cycle.
FT CHAIN 1..562
FT /note="Malate synthase"
FT /id="PRO_0000430876"
FT MOTIF 560..562
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000305"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT ACT_SITE 463
FT /note="Proton donor"
FT /evidence="ECO:0000305"
SQ SEQUENCE 562 AA; 63887 MW; F8FAB0D5F5E08049 CRC64;
MELETSVYRP NVAVYDSPDG VEVRGRYDQI FAKILTREAL SFVAELQREF RGHVKYAMEC
RREARRRYNS GAVPGFDPST KFIRDGDWSC ASVPPAVADR RVEITGPVER KMIINALNSG
AKVFMADFED ALSPSWENLM RGHVNLKDAV DGSITFHDKS RNRVYKLNDQ TAKLFVRPRG
WHLPEAHILI DGEPATGCLV DFGLYFFHNY AKFRQTQGSG FGPFFYLPKM EHSREAKIWN
SVFERAEKMA GIERGSIRAT VLIETLPAVF QMNEILYELR DHSVGLNCGR WDYIFSYVKT
FQAHPDRLLP DRVLVGMGQH FMRSYSDLLI RTCHKRGVHA MGGMAAQIPI RDDPKANEMA
LDLVRKDKLR EVRAGHDGTW AAHPGLIPIC MEAFTGHMGK SPNQIKSVKR EDAAAITEED
LLQIPRGVRT LEGLRLNTRV GIQYLAAWLT GSGSVPLYNL MEDAATAEIS RVQNWQWIRY
GVELDGDGLG VRVSKELFGR VVEEEMERIE KEVGKDKFKN GMYKEACKMF TKQCTAPELD
DFLTLAVYNH IVAHYPINVS RL
