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Protein

Malate synthase G

Gene

glcB

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA.UniRule annotation

Catalytic activityi

Acetyl-CoA + H2O + glyoxylate = (S)-malate + CoA.UniRule annotation1 Publication

Cofactori

Mg2+UniRule annotation1 PublicationNote: Mg(2+). Co(2+) or Mn2+ could partially replace magnesium.UniRule annotation1 Publication

Enzyme regulationi

Inhibited by oxalate, glycolate and ATP.1 Publication

Kineticsi

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

pH dependencei

Optimum pH is 7.6.1 Publication

Temperature dependencei

Optimum temperature is 43 degrees Celsius.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei135 – 1351Acetyl-CoA; via carbonyl oxygenUniRule annotation
Binding sitei292 – 2921Acetyl-CoAUniRule annotation
Binding sitei329 – 3291Acetyl-CoAUniRule annotation
Active sitei356 – 3561Proton acceptorUniRule annotation
Binding sitei356 – 3561GlyoxylateUniRule annotation
Metal bindingi447 – 4471MagnesiumUniRule annotation
Binding sitei447 – 4471GlyoxylateUniRule annotation
Metal bindingi475 – 4751MagnesiumUniRule annotation
Binding sitei556 – 5561Acetyl-CoA; via carbonyl oxygenUniRule annotation
Active sitei647 – 6471Proton donorUniRule annotation

GO - Molecular functioni

  1. malate synthase activity Source: UniProtKB-HAMAP
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. glyoxylate cycle Source: UniProtKB-HAMAP
  2. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Glyoxylate bypass, Tricarboxylic acid cycle

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi2.3.3.9. 960.
UniPathwayiUPA00703; UER00720.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate synthase GUniRule annotation (EC:2.3.3.9UniRule annotation)
Gene namesi
Name:glcBUniRule annotation
Synonyms:aceB
Ordered Locus Names:Cgl2329, cg2559
OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Taxonomic identifieri196627 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000001009 Componenti: Chromosome UP000000582 Componenti: Chromosome

Subcellular locationi

  1. Cytoplasm UniRule annotation1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 739738Malate synthase GPRO_0000166885Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei633 – 6331Cysteine sulfenic acid (-SOH)UniRule annotation

Keywords - PTMi

Oxidation

Interactioni

Subunit structurei

Monomer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi196627.cg2559.

Structurei

3D structure databases

ProteinModelPortaliP42450.
SMRiP42450. Positions 20-738.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni142 – 1432Acetyl-CoA bindingUniRule annotation
Regioni472 – 4754Glyoxylate bindingUniRule annotation

Sequence similaritiesi

Belongs to the malate synthase family. GlcB subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG2225.
KOiK01638.
OMAiPKMHGPD.
OrthoDBiEOG6HJ286.

Family and domain databases

Gene3Di2.170.170.11. 2 hits.
HAMAPiMF_00641. Malate_synth_G.
InterProiIPR011076. Malate_synth-like.
IPR023310. Malate_synth_G_beta_sub_dom.
IPR001465. Malate_synthase.
IPR006253. Malate_synthG.
[Graphical view]
PfamiPF01274. Malate_synthase. 1 hit.
[Graphical view]
SUPFAMiSSF51645. SSF51645. 1 hit.
TIGRFAMsiTIGR01345. malate_syn_G. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P42450-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEQELLSAQ TADNAGTDST ERVDAGGMQV AKVLYDFVTE AVLPRVGVDA
60 70 80 90 100
EKFWSGFAAI ARDLTPRNRE LLARRDELQM LIDDYHRNNS GTIDQEAYED
110 120 130 140 150
FLKEIGYLVE EPEAAEIRTQ NVDTEISSTA GPQLVVPILN ARFALNAANA
160 170 180 190 200
RWGSLYDALY GTNAIPETDG AEKGKEYNPV RGQKVIEWGR EFLDSVVPLD
210 220 230 240 250
GASHADVEKY NITDGKLAAH IGDSVYRLKN RESYRGFTGN FLDPEAILLE
260 270 280 290 300
TNGLHIELQI DPVHPIGKAD KTGLKDIVLE SAITTIMDFE DSVAAVDAED
310 320 330 340 350
KTLGYSNWFG LNTGELKEEM SKNGRIFTRE LNKDRVYIGR NGTELVLHGR
360 370 380 390 400
SLLFVRNVGH LMQNPSILID GEEIFEGIMD AVLTTVCAIP GIAPQNKMRN
410 420 430 440 450
SRKGSIYIVK PKQHGPEEVA FTNELFGRVE DLLDLPRHTL KVGVMDEERR
460 470 480 490 500
TSVNLDASIM EVADRLAFIN TGFLDRTGDE IHTSMEAGAM VRKADMQTAP
510 520 530 540 550
WKQAYENNNV DAGIQRGLPG KAQIGKGMWA MTELMAEMLE KKIGQPREGA
560 570 580 590 600
NTAWVPSPTG ATLHATHYHL VDVFKVQDEL RAAGRRDSLR NILTIPTAPN
610 620 630 640 650
TNWSEEEKKE EMDNNCQSIL GYVVRWVEHG VGCSKVPDIH DIDLMEDRAT
660 670 680 690 700
LRISSQMLAN WIRHDVVSKE QVLESLERMA VVVDKQNAGD EAYRDMAPNY
710 720 730
DASLAFQAAK DLIFEGTKSP SGYTEPILHA RRREFKAKN
Length:739
Mass (Da):82,363
Last modified:January 23, 2007 - v2
Checksum:iDE9AC15F65CCC8EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78491 Genomic DNA. Translation: CAA55243.1.
L27123 Genomic DNA. Translation: AAA68074.1.
BA000036 Genomic DNA. Translation: BAB99722.1.
BX927154 Genomic DNA. Translation: CAF20673.1.
PIRiI40715.
RefSeqiNP_601530.1. NC_003450.3.
WP_011015044.1. NC_006958.1.
YP_226574.1. NC_006958.1.

Genome annotation databases

EnsemblBacteriaiBAB99722; BAB99722; BAB99722.
GeneIDi1020280.
23502779.
KEGGicgb:cg2559.
cgl:NCgl2247.
PATRICi21496662. VBICorGlu203724_2263.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78491 Genomic DNA. Translation: CAA55243.1.
L27123 Genomic DNA. Translation: AAA68074.1.
BA000036 Genomic DNA. Translation: BAB99722.1.
BX927154 Genomic DNA. Translation: CAF20673.1.
PIRiI40715.
RefSeqiNP_601530.1. NC_003450.3.
WP_011015044.1. NC_006958.1.
YP_226574.1. NC_006958.1.

3D structure databases

ProteinModelPortaliP42450.
SMRiP42450. Positions 20-738.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196627.cg2559.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB99722; BAB99722; BAB99722.
GeneIDi1020280.
23502779.
KEGGicgb:cg2559.
cgl:NCgl2247.
PATRICi21496662. VBICorGlu203724_2263.

Phylogenomic databases

eggNOGiCOG2225.
KOiK01638.
OMAiPKMHGPD.
OrthoDBiEOG6HJ286.

Enzyme and pathway databases

UniPathwayiUPA00703; UER00720.
BRENDAi2.3.3.9. 960.

Family and domain databases

Gene3Di2.170.170.11. 2 hits.
HAMAPiMF_00641. Malate_synth_G.
InterProiIPR011076. Malate_synth-like.
IPR023310. Malate_synth_G_beta_sub_dom.
IPR001465. Malate_synthase.
IPR006253. Malate_synthG.
[Graphical view]
PfamiPF01274. Malate_synthase. 1 hit.
[Graphical view]
SUPFAMiSSF51645. SSF51645. 1 hit.
TIGRFAMsiTIGR01345. malate_syn_G. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Entry informationi

Entry nameiMASZ_CORGL
AccessioniPrimary (citable) accession number: P42450
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.