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P37330 (MASZ_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Malate synthase G

Short name=MSG
EC=2.3.3.9
Gene names
Name:glcB
Synonyms:glc
Ordered Locus Names:b2976, JW2943
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length723 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA. Ref.1 Ref.4 Ref.5

Catalytic activity

Acetyl-CoA + H2O + glyoxylate = (S)-malate + CoA. HAMAP-Rule MF_00641

Cofactor

Magnesium. Ref.7

Pathway

Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. HAMAP-Rule MF_00641

Subunit structure

Monomer. Ref.1 Ref.7 Ref.9

Subcellular location

Cytoplasm HAMAP-Rule MF_00641.

Induction

By glycolate. Ref.1 Ref.4 Ref.6

Disruption phenotype

Cells lacking this gene are unable to oxidize glyoxylate. Ref.4

Sequence similarities

Belongs to the malate synthase family. GlcB subfamily.

Biophysicochemical properties

Kinetic parameters:

Kcat is 48.1 sec(-1) for glyoxylate (at pH 8 and 37 degrees Celsius).

KM=9 µM for acetyl-CoA (at pH 8 and 37 degrees Celsius) Ref.8

KM=21 µM for glyoxylate (at pH 8 and 37 degrees Celsius)

Vmax=36.1 µmol/min/mg enzyme (at pH 8 and 37 degrees Celsius)

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 723722Malate synthase G HAMAP-Rule MF_00641
PRO_0000166886

Regions

Region125 – 1262Acetyl-CoA binding HAMAP-Rule MF_00641
Region452 – 4554Glyoxylate binding HAMAP-Rule MF_00641

Sites

Active site3381Proton acceptor Ref.7 Ref.8
Active site6311Proton donor Ref.7 Ref.8
Metal binding4271Magnesium
Metal binding4551Magnesium
Binding site1181Acetyl-CoA; via carbonyl oxygen
Binding site2741Acetyl-CoA
Binding site3111Acetyl-CoA
Binding site3381Glyoxylate
Binding site4271Glyoxylate
Binding site5361Acetyl-CoA; via carbonyl oxygen

Amino acid modifications

Modified residue6171Cysteine sulfenic acid (-SOH) HAMAP-Rule MF_00641
Modified residue6881Cysteine sulfenic acid (-SOH) HAMAP-Rule MF_00641

Experimental info

Mutagenesis3381R → K: Has a specific activity which is only 6.6% of the wild-type activity. Ref.8
Mutagenesis6171C → S: Affinity binding for acetyl-CoA is more than five times greater than that of wild-type, although its specific activity is comparable. Ref.8
Mutagenesis6311D → N: Absence of malate synthase activity. Ref.8

Secondary structure

.................................................................................................................................... 723
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P37330 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 820F177D3FE02632

FASTA72380,489
        10         20         30         40         50         60 
MSQTITQSRL RIDANFKRFV DEEVLPGTGL DAAAFWRNFD EIVHDLAPEN RQLLAERDRI 

        70         80         90        100        110        120 
QAALDEWHRS NPGPVKDKAA YKSFLRELGY LVPQPERVTV ETTGIDSEIT SQAGPQLVVP 

       130        140        150        160        170        180 
AMNARYALNA ANARWGSLYD ALYGSDIIPQ EGAMVSGYDP QRGEQVIAWV RRFLDESLPL 

       190        200        210        220        230        240 
ENGSYQDVVA FKVVDKQLRI QLKNGKETTL RTPAQFVGYR GDAAAPTCIL LKNNGLHIEL 

       250        260        270        280        290        300 
QIDANGRIGK DDPAHINDVI VEAAISTILD CEDSVAAVDA EDKILLYRNL LGLMQGTLQE 

       310        320        330        340        350        360 
KMEKNGRQIV RKLNDDRHYT AADGSEISLH GRSLLFIRNV GHLMTIPVIW DSEGNEIPEG 

       370        380        390        400        410        420 
ILDGVMTGAI ALYDLKVQKN SRTGSVYIVK PKMHGPQEVA FANKLFTRIE TMLGMAPNTL 

       430        440        450        460        470        480 
KMGIMDEERR TSLNLRSCIA QARNRVAFIN TGFLDRTGDE MHSVMEAGPM LRKNQMKSTP 

       490        500        510        520        530        540 
WIKAYERNNV LSGLFCGLRG KAQIGKGMWA MPDLMADMYS QKGDQLRAGA NTAWVPSPTA 

       550        560        570        580        590        600 
ATLHALHYHQ TNVQSVQANI AQTEFNAEFE PLLDDLLTIP VAENANWSAQ EIQQELDNNV 

       610        620        630        640        650        660 
QGILGYVVRW VEQGIGCSKV PDIHNVALME DRATLRISSQ HIANWLRHGI LTKEQVQASL 

       670        680        690        700        710        720 
ENMAKVVDQQ NAGDPAYRPM AGNFANSCAF KAASDLIFLG VKQPNGYTEP LLHAWRLREK 


ESH 

« Hide

References

« Hide 'large scale' references
[1]"Molecular characterization of Escherichia coli malate synthase G. Differentiation with the malate synthase A isoenzyme."
Molina I., Badia J., Aguilar J.T., Pellicer M.T., Baldoma L.
Eur. J. Biochem. 224:541-548(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13, FUNCTION, SUBUNIT, INDUCTION, NOMENCLATURE.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Regulation of glyoxylate metabolism in Escherichia coli K-12."
Ornston L.N., Ornston M.K.
J. Bacteriol. 98:1098-1108(1969) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION.
[5]"Demonstration of 2 malate synthases in Escherichia coli."
Falmagne P., Vanderwinkel E., Wiame J.M.
Biochim. Biophys. Acta 99:246-258(1965) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Cross-induction of glc and ace operons of Escherichia coli attributable to pathway intersection. Characterization of the glc promoter."
Pellicer M.T., Fernandez C., Badia J., Aguilar J., Lin E.C., Baldom L.
J. Biol. Chem. 274:1745-1752(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[7]"Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0-A resolution: mechanistic implications."
Howard B.R., Endrizzi J.A., Remington S.J.
Biochemistry 39:3156-3168(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND MAGNESIUM ION, ACTIVE SITE, COFACTOR, REACTION MECHANISM, SUBUNIT.
[8]"Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 A resolution."
Anstrom D.M., Kallio K., Remington S.J.
Protein Sci. 12:1822-1832(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 3-722 IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM ION, MUTAGENESIS OF ARG-338; CYS-617 AND ASP-631, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES.
[9]"Solution NMR-derived global fold of a monomeric 82-kDa enzyme."
Tugarinov V., Choy W.Y., Orekhov V.Y., Kay L.E.
Proc. Natl. Acad. Sci. U.S.A. 102:622-627(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 3-722, SUBUNIT.
[10]"Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints."
Grishaev A., Tugarinov V., Kay L.E., Trewhella J., Bax A.
J. Biomol. NMR 40:95-106(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 3-723.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X74547 Genomic DNA. Translation: CAA52639.1.
U28377 Genomic DNA. Translation: AAA69143.1.
U00096 Genomic DNA. Translation: AAC76012.1.
AP009048 Genomic DNA. Translation: BAE77036.1.
PIRS51788.
RefSeqNP_417450.1. NC_000913.3.
YP_491172.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8CX-ray2.00A3-723[»]
1P7TX-ray1.95A/B3-722[»]
1Y8BNMR-A3-722[»]
2JQXNMR-A3-723[»]
ProteinModelPortalP37330.
SMRP37330. Positions 1-723.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9761N.
IntActP37330. 6 interactions.
MINTMINT-1248166.
STRING511145.b2976.

Proteomic databases

PaxDbP37330.
PRIDEP37330.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76012; AAC76012; b2976.
BAE77036; BAE77036; BAE77036.
GeneID12930245.
948857.
KEGGecj:Y75_p2904.
eco:b2976.
PATRIC32121366. VBIEscCol129921_3070.

Organism-specific databases

EchoBASEEB4141.
EcoGeneEG20080. glcB.

Phylogenomic databases

eggNOGCOG2225.
HOGENOMHOG000220740.
KOK01638.
OMAIQIDAND.
OrthoDBEOG6HJ286.
PhylomeDBP37330.
ProtClustDBPRK02999.

Enzyme and pathway databases

BioCycEcoCyc:MALSYNG-MONOMER.
ECOL316407:JW2943-MONOMER.
MetaCyc:MALSYNG-MONOMER.
UniPathwayUPA00703; UER00720.

Gene expression databases

GenevestigatorP37330.

Family and domain databases

Gene3D2.170.170.11. 2 hits.
HAMAPMF_00641. Malate_synth_G.
InterProIPR011076. Malate_synth-like.
IPR023310. Malate_synth_G_beta_sub_dom.
IPR001465. Malate_synthase.
IPR006253. Malate_synthG.
[Graphical view]
PfamPF01274. Malate_synthase. 1 hit.
[Graphical view]
SUPFAMSSF51645. SSF51645. 1 hit.
TIGRFAMsTIGR01345. malate_syn_G. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP37330.
PROP37330.

Entry information

Entry nameMASZ_ECOLI
AccessionPrimary (citable) accession number: P37330
Secondary accession number(s): Q2M9M0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene