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Protein

Malate synthase

Gene

MLS

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Does not seem to be essential for lipid utilization and gluconeogenesis in seedlings.1 Publication

Catalytic activityi

Acetyl-CoA + H2O + glyoxylate = (S)-malate + CoA.1 Publication

Pathwayi: glyoxylate cycle

This protein is involved in step 2 of the subpathway that synthesizes (S)-malate from isocitrate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Isocitrate lyase (ICL)
  2. Malate synthase, Malate synthase (MLS), Malate synthase, Malate synthase
This subpathway is part of the pathway glyoxylate cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-malate from isocitrate, the pathway glyoxylate cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei177 – 1771Proton acceptorCurated
Active sitei463 – 4631Proton donorCurated

GO - Molecular functioni

  • malate synthase activity Source: TAIR

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Glyoxylate bypass, Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciARA:GQT-1825-MONOMER.
MetaCyc:AT5G03860-MONOMER.
UniPathwayiUPA00703; UER00720.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate synthase1 Publication (EC:2.3.3.91 Publication)
Gene namesi
Name:MLS1 Publication
Ordered Locus Names:At5g03860Imported
ORF Names:F8F6.70Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G03860.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Glyoxysome, Peroxisome

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth conditions, but the frequency of mutant seedlings to establish into plantlets with true leaves is decreased under short day conditions.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 562562Malate synthasePRO_0000430876Add
BLAST

Proteomic databases

PaxDbiQ9LZC3.
PRIDEiQ9LZC3.

Expressioni

Developmental stagei

Expressed from 1 to 5 days after seed imbibition (at protein level).1 Publication

Gene expression databases

GenevisibleiQ9LZC3. AT.

Interactioni

Protein-protein interaction databases

BioGridi16966. 1 interaction.
STRINGi3702.AT5G03860.1.

Structurei

3D structure databases

ProteinModelPortaliQ9LZC3.
SMRiQ9LZC3. Positions 31-548.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi560 – 5623Microbody targeting signalCurated

Sequence similaritiesi

Belongs to the malate synthase family.Curated

Phylogenomic databases

eggNOGiKOG1261. Eukaryota.
COG2225. LUCA.
HOGENOMiHOG000238464.
InParanoidiQ9LZC3.
KOiK01638.
OMAiECRRVEI.
PhylomeDBiQ9LZC3.

Family and domain databases

InterProiIPR011076. Malate_synth-like.
IPR006252. Malate_synthA.
IPR001465. Malate_synthase.
IPR019830. Malate_synthase_CS.
[Graphical view]
PfamiPF01274. Malate_synthase. 1 hit.
[Graphical view]
PIRSFiPIRSF001363. Malate_synth. 1 hit.
SUPFAMiSSF51645. SSF51645. 1 hit.
TIGRFAMsiTIGR01344. malate_syn_A. 1 hit.
PROSITEiPS00510. MALATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9LZC3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELETSVYRP NVAVYDSPDG VEVRGRYDQI FAKILTREAL SFVAELQREF
60 70 80 90 100
RGHVKYAMEC RREARRRYNS GAVPGFDPST KFIRDGDWSC ASVPPAVADR
110 120 130 140 150
RVEITGPVER KMIINALNSG AKVFMADFED ALSPSWENLM RGHVNLKDAV
160 170 180 190 200
DGSITFHDKS RNRVYKLNDQ TAKLFVRPRG WHLPEAHILI DGEPATGCLV
210 220 230 240 250
DFGLYFFHNY AKFRQTQGSG FGPFFYLPKM EHSREAKIWN SVFERAEKMA
260 270 280 290 300
GIERGSIRAT VLIETLPAVF QMNEILYELR DHSVGLNCGR WDYIFSYVKT
310 320 330 340 350
FQAHPDRLLP DRVLVGMGQH FMRSYSDLLI RTCHKRGVHA MGGMAAQIPI
360 370 380 390 400
RDDPKANEMA LDLVRKDKLR EVRAGHDGTW AAHPGLIPIC MEAFTGHMGK
410 420 430 440 450
SPNQIKSVKR EDAAAITEED LLQIPRGVRT LEGLRLNTRV GIQYLAAWLT
460 470 480 490 500
GSGSVPLYNL MEDAATAEIS RVQNWQWIRY GVELDGDGLG VRVSKELFGR
510 520 530 540 550
VVEEEMERIE KEVGKDKFKN GMYKEACKMF TKQCTAPELD DFLTLAVYNH
560
IVAHYPINVS RL
Length:562
Mass (Da):63,887
Last modified:October 1, 2000 - v1
Checksum:iF8FAB0D5F5E08049
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005235 Genomic DNA. Translation: BAB08612.1.
AL162873 Genomic DNA. Translation: CAB85506.1.
CP002688 Genomic DNA. Translation: AED90663.1.
CP002688 Genomic DNA. Translation: AED90664.1.
AF360126 mRNA. Translation: AAK25836.1.
AY051027 mRNA. Translation: AAK93704.1.
PIRiT48413.
RefSeqiNP_001190219.1. NM_001203290.1.
NP_196006.1. NM_120467.3.
UniGeneiAt.4884.

Genome annotation databases

EnsemblPlantsiAT5G03860.1; AT5G03860.1; AT5G03860.
AT5G03860.2; AT5G03860.2; AT5G03860.
GeneIDi831690.
GrameneiAT5G03860.1; AT5G03860.1; AT5G03860.
AT5G03860.2; AT5G03860.2; AT5G03860.
KEGGiath:AT5G03860.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005235 Genomic DNA. Translation: BAB08612.1.
AL162873 Genomic DNA. Translation: CAB85506.1.
CP002688 Genomic DNA. Translation: AED90663.1.
CP002688 Genomic DNA. Translation: AED90664.1.
AF360126 mRNA. Translation: AAK25836.1.
AY051027 mRNA. Translation: AAK93704.1.
PIRiT48413.
RefSeqiNP_001190219.1. NM_001203290.1.
NP_196006.1. NM_120467.3.
UniGeneiAt.4884.

3D structure databases

ProteinModelPortaliQ9LZC3.
SMRiQ9LZC3. Positions 31-548.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi16966. 1 interaction.
STRINGi3702.AT5G03860.1.

Proteomic databases

PaxDbiQ9LZC3.
PRIDEiQ9LZC3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G03860.1; AT5G03860.1; AT5G03860.
AT5G03860.2; AT5G03860.2; AT5G03860.
GeneIDi831690.
GrameneiAT5G03860.1; AT5G03860.1; AT5G03860.
AT5G03860.2; AT5G03860.2; AT5G03860.
KEGGiath:AT5G03860.

Organism-specific databases

TAIRiAT5G03860.

Phylogenomic databases

eggNOGiKOG1261. Eukaryota.
COG2225. LUCA.
HOGENOMiHOG000238464.
InParanoidiQ9LZC3.
KOiK01638.
OMAiECRRVEI.
PhylomeDBiQ9LZC3.

Enzyme and pathway databases

UniPathwayiUPA00703; UER00720.
BioCyciARA:GQT-1825-MONOMER.
MetaCyc:AT5G03860-MONOMER.

Miscellaneous databases

PROiQ9LZC3.

Gene expression databases

GenevisibleiQ9LZC3. AT.

Family and domain databases

InterProiIPR011076. Malate_synth-like.
IPR006252. Malate_synthA.
IPR001465. Malate_synthase.
IPR019830. Malate_synthase_CS.
[Graphical view]
PfamiPF01274. Malate_synthase. 1 hit.
[Graphical view]
PIRSFiPIRSF001363. Malate_synth. 1 hit.
SUPFAMiSSF51645. SSF51645. 1 hit.
TIGRFAMsiTIGR01344. malate_syn_A. 1 hit.
PROSITEiPS00510. MALATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones."
    Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S.
    DNA Res. 4:215-230(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Lipid utilization, gluconeogenesis, and seedling growth in Arabidopsis mutants lacking the glyoxylate cycle enzyme malate synthase."
    Cornah J.E., Germain V., Ward J.L., Beale M.H., Smith S.M.
    J. Biol. Chem. 279:42916-42923(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
  6. "Peroxisome-associated matrix protein degradation in Arabidopsis."
    Lingard M.J., Monroe-Augustus M., Bartel B.
    Proc. Natl. Acad. Sci. U.S.A. 106:4561-4566(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiMASY_ARATH
AccessioniPrimary (citable) accession number: Q9LZC3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 29, 2014
Last sequence update: October 1, 2000
Last modified: February 17, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.