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P37330 (MASZ_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 119. 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
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 lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

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

Accounts for almost the entire malate-synthesizing activity in cells metabolizing glyoxylate. HAMAP-Rule MF_00641

Catalytic activity

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

Cofactor

Magnesium.

Pathway

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

Subunit structure

Monomer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00641.

Sequence similarities

Belongs to the malate synthase family. GlcB subfamily.

Ontologies

Keywords
   Biological processGlyoxylate bypass
Tricarboxylic acid cycle
   Cellular componentCytoplasm
   LigandMagnesium
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglyoxylate catabolic process

Inferred from expression pattern PubMed 4892366. Source: EcoCyc

glyoxylate cycle

Inferred from electronic annotation. Source: HAMAP

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmalate synthase activity

Inferred from direct assay PubMed 4591144. Source: EcoCyc

Complete GO annotation...

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

Sites

Active site3381Proton acceptor
Active site6311Proton donor

Secondary structure

1 .................................................................................................................................... 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.
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 277:1453-1474(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]"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).
+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_000913.2.
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...

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.
OMASQFIENE.
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]
PANTHERPTHR21631:SF1. PTHR21631:SF1. 1 hit.
PfamPF01274. Malate_synthase. 1 hit.
[Graphical view]
SUPFAMSSF51645. Malat_synth_like. 1 hit.
TIGRFAMsTIGR01345. malate_syn_G. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP37330.

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: May 29, 2013
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents