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P42450 (MASZ_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

EC=2.3.3.9
Gene names
Name:glcB
Synonyms:aceB
Ordered Locus Names:Cgl2329, cg2559
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length739 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 By similarity. Ref.1

Catalytic activity

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

Cofactor

Magnesium. Cobalt or Mnaganese could partially replace magnesium. Ref.1

Enzyme regulation

Inhibited by oxalate, glycolate and ATP. Ref.1

Pathway

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

Subunit structure

Monomer. Ref.1

Subcellular location

Cytoplasm Ref.1.

Disruption phenotype

Cells lacking this gene show the absence of malate synthase activity and to the inability to grow on acetate. Ref.1

Sequence similarities

Belongs to the malate synthase family. GlcB subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=12 µM for acetyl-CoA (at pH 7.6 and 30 degrees Celsius) Ref.1

KM=30 µM for glyoxylate (at pH 7.6 and 30 degrees Celsius)

pH dependence:

Optimum pH is 7.6.

Temperature dependence:

Optimum temperature is 43 degrees Celsius.

Ontologies

Keywords
   Biological processGlyoxylate bypass
Tricarboxylic acid cycle
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionTransferase
   PTMOxidation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglyoxylate cycle

Inferred from electronic annotation. Source: UniProtKB-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 electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 739738Malate synthase G HAMAP-Rule MF_00641
PRO_0000166885

Regions

Region142 – 1432Acetyl-CoA binding By similarity
Region472 – 4754Glyoxylate binding By similarity

Sites

Active site3561Proton acceptor By similarity
Active site6471Proton donor By similarity
Metal binding4471Magnesium By similarity
Metal binding4751Magnesium By similarity
Binding site1351Acetyl-CoA; via carbonyl oxygen By similarity
Binding site2921Acetyl-CoA By similarity
Binding site3291Acetyl-CoA By similarity
Binding site3561Glyoxylate By similarity
Binding site4471Glyoxylate By similarity
Binding site5561Acetyl-CoA; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue6331Cysteine sulfenic acid (-SOH) By similarity

Sequences

Sequence LengthMass (Da)Tools
P42450 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: DE9AC15F65CCC8EB

FASTA73982,363
        10         20         30         40         50         60 
MTEQELLSAQ TADNAGTDST ERVDAGGMQV AKVLYDFVTE AVLPRVGVDA EKFWSGFAAI 

        70         80         90        100        110        120 
ARDLTPRNRE LLARRDELQM LIDDYHRNNS GTIDQEAYED FLKEIGYLVE EPEAAEIRTQ 

       130        140        150        160        170        180 
NVDTEISSTA GPQLVVPILN ARFALNAANA RWGSLYDALY GTNAIPETDG AEKGKEYNPV 

       190        200        210        220        230        240 
RGQKVIEWGR EFLDSVVPLD GASHADVEKY NITDGKLAAH IGDSVYRLKN RESYRGFTGN 

       250        260        270        280        290        300 
FLDPEAILLE TNGLHIELQI DPVHPIGKAD KTGLKDIVLE SAITTIMDFE DSVAAVDAED 

       310        320        330        340        350        360 
KTLGYSNWFG LNTGELKEEM SKNGRIFTRE LNKDRVYIGR NGTELVLHGR SLLFVRNVGH 

       370        380        390        400        410        420 
LMQNPSILID GEEIFEGIMD AVLTTVCAIP GIAPQNKMRN SRKGSIYIVK PKQHGPEEVA 

       430        440        450        460        470        480 
FTNELFGRVE DLLDLPRHTL KVGVMDEERR TSVNLDASIM EVADRLAFIN TGFLDRTGDE 

       490        500        510        520        530        540 
IHTSMEAGAM VRKADMQTAP WKQAYENNNV DAGIQRGLPG KAQIGKGMWA MTELMAEMLE 

       550        560        570        580        590        600 
KKIGQPREGA NTAWVPSPTG ATLHATHYHL VDVFKVQDEL RAAGRRDSLR NILTIPTAPN 

       610        620        630        640        650        660 
TNWSEEEKKE EMDNNCQSIL GYVVRWVEHG VGCSKVPDIH DIDLMEDRAT LRISSQMLAN 

       670        680        690        700        710        720 
WIRHDVVSKE QVLESLERMA VVVDKQNAGD EAYRDMAPNY DASLAFQAAK DLIFEGTKSP 

       730 
SGYTEPILHA RRREFKAKN 

« Hide

References

« Hide 'large scale' references
[1]"Malate synthase from Corynebacterium glutamicum: sequence analysis of the gene and biochemical characterization of the enzyme."
Reinscheid D.J., Eikmanns B.J., Sahm H.
Microbiology 140:3099-3108(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, COFACTOR, SUBUNIT.
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"Molecular characterization of aceB, a gene encoding malate synthase in Corynebacterium glutamicum."
Lee H.S., Sinskey A.J.
J. Microbiol. Biotechnol. 4:256-263(1994)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613.
[3]"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
Ikeda M., Nakagawa S.
Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[4]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78491 Genomic DNA. Translation: CAA55243.1.
L27123 Genomic DNA. Translation: AAA68074.1.
BA000036 Genomic DNA. Translation: BAB99722.1.
BX927154 Genomic DNA. Translation: CAF20673.1.
PIRI40715.
RefSeqNP_601530.1. NC_003450.3.
YP_226574.1. NC_006958.1.

3D structure databases

ProteinModelPortalP42450.
SMRP42450. Positions 20-738.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196627.cg2559.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB99722; BAB99722; BAB99722.
CAF20673; CAF20673; cg2559.
GeneID1020280.
3345106.
KEGGcgb:cg2559.
cgl:NCgl2247.
PATRIC21496662. VBICorGlu203724_2263.

Phylogenomic databases

eggNOGCOG2225.
KOK01638.
OMAPKMHGPD.
OrthoDBEOG6HJ286.
ProtClustDBPRK02999.

Enzyme and pathway databases

BRENDA2.3.3.9. 1648.
UniPathwayUPA00703; UER00720.

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...

Entry information

Entry nameMASZ_CORGL
AccessionPrimary (citable) accession number: P42450
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 95 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways