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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

    Pathway: 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 (aceA)
    2. Malate synthase G (glcB)
    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
    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

    GO - Biological processi

    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 lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
    ProteomesiUP000000582 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm UniRule annotation1 Publication

    GO - Cellular componenti

    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

    Expressioni

    Inductioni

    Activated by RamA and repressed by RamB.2 Publications

    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.
    CAF20673; CAF20673; cg2559.
    GeneIDi1020280.
    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.
    CAF20673; CAF20673; cg2559.
    GeneIDi1020280.
    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.
    5. "RamB, a novel transcriptional regulator of genes involved in acetate metabolism of Corynebacterium glutamicum."
      Gerstmeir R., Cramer A., Dangel P., Schaffer S., Eikmanns B.J.
      J. Bacteriol. 186:2798-2809(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
      Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
    6. "Identification of RamA, a novel LuxR-type transcriptional regulator of genes involved in acetate metabolism of Corynebacterium glutamicum."
      Cramer A., Gerstmeir R., Schaffer S., Bott M., Eikmanns B.J.
      J. Bacteriol. 188:2554-2567(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
      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: June 24, 2015
    This is version 106 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.