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P42450

- MASZ_CORGL

UniProt

P42450 - MASZ_CORGL

Protein

Malate synthase G

Gene

glcB

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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.1 PublicationUniRule annotation

    Cofactori

    Magnesium. Cobalt or Mnaganese could partially replace magnesium.1 PublicationUniRule annotation

    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

    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. 1648.
    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
    ProteomesiUP000000582: Chromosome, UP000001009: Chromosome

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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.1 PublicationUniRule annotation

    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.
    OMAiSTIMDFE.
    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

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    MTEQELLSAQ TADNAGTDST ERVDAGGMQV AKVLYDFVTE AVLPRVGVDA    50
    EKFWSGFAAI ARDLTPRNRE LLARRDELQM LIDDYHRNNS GTIDQEAYED 100
    FLKEIGYLVE EPEAAEIRTQ NVDTEISSTA GPQLVVPILN ARFALNAANA 150
    RWGSLYDALY GTNAIPETDG AEKGKEYNPV RGQKVIEWGR EFLDSVVPLD 200
    GASHADVEKY NITDGKLAAH IGDSVYRLKN RESYRGFTGN FLDPEAILLE 250
    TNGLHIELQI DPVHPIGKAD KTGLKDIVLE SAITTIMDFE DSVAAVDAED 300
    KTLGYSNWFG LNTGELKEEM SKNGRIFTRE LNKDRVYIGR NGTELVLHGR 350
    SLLFVRNVGH LMQNPSILID GEEIFEGIMD AVLTTVCAIP GIAPQNKMRN 400
    SRKGSIYIVK PKQHGPEEVA FTNELFGRVE DLLDLPRHTL KVGVMDEERR 450
    TSVNLDASIM EVADRLAFIN TGFLDRTGDE IHTSMEAGAM VRKADMQTAP 500
    WKQAYENNNV DAGIQRGLPG KAQIGKGMWA MTELMAEMLE KKIGQPREGA 550
    NTAWVPSPTG ATLHATHYHL VDVFKVQDEL RAAGRRDSLR NILTIPTAPN 600
    TNWSEEEKKE EMDNNCQSIL GYVVRWVEHG VGCSKVPDIH DIDLMEDRAT 650
    LRISSQMLAN WIRHDVVSKE QVLESLERMA VVVDKQNAGD EAYRDMAPNY 700
    DASLAFQAAK DLIFEGTKSP SGYTEPILHA RRREFKAKN 739
    Length:739
    Mass (Da):82,363
    Last modified:January 23, 2007 - v2
    Checksum:iDE9AC15F65CCC8EB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi I40715.
    RefSeqi NP_601530.1. NC_003450.3.
    WP_011015044.1. NC_006958.1.
    YP_226574.1. NC_006958.1.

    3D structure databases

    ProteinModelPortali P42450.
    SMRi P42450. Positions 20-738.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 196627.cg2559.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB99722 ; BAB99722 ; BAB99722 .
    CAF20673 ; CAF20673 ; cg2559 .
    GeneIDi 1020280.
    KEGGi cgb:cg2559.
    cgl:NCgl2247.
    PATRICi 21496662. VBICorGlu203724_2263.

    Phylogenomic databases

    eggNOGi COG2225.
    KOi K01638.
    OMAi STIMDFE.
    OrthoDBi EOG6HJ286.

    Enzyme and pathway databases

    UniPathwayi UPA00703 ; UER00720 .
    BRENDAi 2.3.3.9. 1648.

    Family and domain databases

    Gene3Di 2.170.170.11. 2 hits.
    HAMAPi MF_00641. Malate_synth_G.
    InterProi IPR011076. Malate_synth-like.
    IPR023310. Malate_synth_G_beta_sub_dom.
    IPR001465. Malate_synthase.
    IPR006253. Malate_synthG.
    [Graphical view ]
    Pfami PF01274. Malate_synthase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51645. SSF51645. 1 hit.
    TIGRFAMsi TIGR01345. malate_syn_G. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 99 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