Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P37330

- MASZ_ECOLI

UniProt

P37330 - MASZ_ECOLI

Protein

Malate synthase G

Gene

glcB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.3 PublicationsUniRule annotation

    Catalytic activityi

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

    Cofactori

    Magnesium.1 PublicationUniRule annotation

    Kineticsi

    Kcat is 48.1 sec(-1) for glyoxylate (at pH 8 and 37 degrees Celsius).

    1. KM=9 µM for acetyl-CoA (at pH 8 and 37 degrees Celsius)1 Publication
    2. KM=21 µM for glyoxylate (at pH 8 and 37 degrees Celsius)1 Publication

    Vmax=36.1 µmol/min/mg enzyme (at pH 8 and 37 degrees Celsius)1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei118 – 1181Acetyl-CoA; via carbonyl oxygen
    Binding sitei274 – 2741Acetyl-CoA
    Binding sitei311 – 3111Acetyl-CoA
    Active sitei338 – 3381Proton acceptor
    Binding sitei338 – 3381Glyoxylate
    Metal bindingi427 – 4271Magnesium
    Binding sitei427 – 4271Glyoxylate
    Metal bindingi455 – 4551Magnesium
    Binding sitei536 – 5361Acetyl-CoA; via carbonyl oxygen
    Active sitei631 – 6311Proton donor

    GO - Molecular functioni

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

    GO - Biological processi

    1. glyoxylate catabolic process Source: EcoCyc
    2. glyoxylate cycle Source: UniProtKB-HAMAP
    3. 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

    BioCyciEcoCyc:MALSYNG-MONOMER.
    ECOL316407:JW2943-MONOMER.
    MetaCyc:MALSYNG-MONOMER.
    UniPathwayiUPA00703; UER00720.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malate synthase GUniRule annotation (EC:2.3.3.9UniRule annotation)
    Short name:
    MSG
    Gene namesi
    Name:glcBUniRule annotation
    Synonyms:glc
    Ordered Locus Names:b2976, JW2943
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG20080. glcB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene are unable to oxidize glyoxylate.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi338 – 3381R → K: Has a specific activity which is only 6.6% of the wild-type activity. 1 Publication
    Mutagenesisi617 – 6171C → S: Affinity binding for acetyl-CoA is more than five times greater than that of wild-type, although its specific activity is comparable. 1 Publication
    Mutagenesisi631 – 6311D → N: Absence of malate synthase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 723722Malate synthase GPRO_0000166886Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei617 – 6171Cysteine sulfenic acid (-SOH)1 PublicationUniRule annotation
    Modified residuei688 – 6881Cysteine sulfenic acid (-SOH)1 PublicationUniRule annotation

    Keywords - PTMi

    Oxidation

    Proteomic databases

    PaxDbiP37330.
    PRIDEiP37330.

    Expressioni

    Inductioni

    By glycolate.3 Publications

    Gene expression databases

    GenevestigatoriP37330.

    Interactioni

    Subunit structurei

    Monomer.4 PublicationsUniRule annotation

    Protein-protein interaction databases

    DIPiDIP-9761N.
    IntActiP37330. 6 interactions.
    MINTiMINT-1248166.
    STRINGi511145.b2976.

    Structurei

    Secondary structure

    1
    723
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 73
    Beta strandi10 – 123
    Helixi14 – 2310
    Helixi25 – 284
    Helixi32 – 7039
    Beta strandi74 – 763
    Helixi78 – 8710
    Helixi107 – 1104
    Beta strandi116 – 1205
    Helixi124 – 1318
    Helixi132 – 1343
    Beta strandi135 – 1373
    Helixi138 – 1436
    Beta strandi145 – 1484
    Beta strandi152 – 1543
    Beta strandi155 – 1573
    Helixi160 – 17718
    Beta strandi180 – 1834
    Helixi185 – 1873
    Beta strandi188 – 1947
    Beta strandi197 – 2026
    Beta strandi207 – 2126
    Helixi213 – 2153
    Beta strandi216 – 2227
    Beta strandi225 – 2339
    Beta strandi236 – 2427
    Helixi249 – 2513
    Beta strandi256 – 2627
    Beta strandi265 – 2728
    Helixi280 – 29415
    Beta strandi299 – 3013
    Turni305 – 3073
    Beta strandi310 – 3123
    Beta strandi317 – 3215
    Beta strandi326 – 3294
    Beta strandi331 – 3333
    Beta strandi334 – 3385
    Beta strandi345 – 3506
    Beta strandi356 – 3583
    Helixi359 – 37719
    Beta strandi382 – 3843
    Beta strandi386 – 3905
    Helixi396 – 41217
    Beta strandi420 – 4267
    Helixi429 – 4324
    Helixi435 – 4406
    Turni441 – 4455
    Beta strandi446 – 4516
    Helixi453 – 46311
    Helixi465 – 4673
    Helixi473 – 4753
    Helixi480 – 49516
    Turni499 – 5013
    Beta strandi502 – 5065
    Helixi515 – 5217
    Helixi523 – 5275
    Beta strandi531 – 5377
    Helixi538 – 55013
    Helixi553 – 5608
    Helixi565 – 57612
    Helixi589 – 61325
    Beta strandi618 – 6214
    Beta strandi627 – 6304
    Helixi632 – 64716
    Turni648 – 6503
    Helixi653 – 67018
    Turni671 – 6733
    Beta strandi674 – 6763
    Turni680 – 6834
    Helixi684 – 6863
    Helixi688 – 69811
    Helixi700 – 7023
    Helixi704 – 7063
    Helixi709 – 72012

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D8CX-ray2.00A1-723[»]
    1P7TX-ray1.95A/B3-723[»]
    1Y8BNMR-A1-723[»]
    2JQXNMR-A1-723[»]
    ProteinModelPortaliP37330.
    SMRiP37330. Positions 1-723.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP37330.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni125 – 1262Acetyl-CoA binding
    Regioni452 – 4554Glyoxylate binding

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG2225.
    HOGENOMiHOG000220740.
    KOiK01638.
    OMAiPANTLKM.
    OrthoDBiEOG6HJ286.
    PhylomeDBiP37330.

    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.

    P37330-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQTITQSRL RIDANFKRFV DEEVLPGTGL DAAAFWRNFD EIVHDLAPEN    50
    RQLLAERDRI QAALDEWHRS NPGPVKDKAA YKSFLRELGY LVPQPERVTV 100
    ETTGIDSEIT SQAGPQLVVP AMNARYALNA ANARWGSLYD ALYGSDIIPQ 150
    EGAMVSGYDP QRGEQVIAWV RRFLDESLPL ENGSYQDVVA FKVVDKQLRI 200
    QLKNGKETTL RTPAQFVGYR GDAAAPTCIL LKNNGLHIEL QIDANGRIGK 250
    DDPAHINDVI VEAAISTILD CEDSVAAVDA EDKILLYRNL LGLMQGTLQE 300
    KMEKNGRQIV RKLNDDRHYT AADGSEISLH GRSLLFIRNV GHLMTIPVIW 350
    DSEGNEIPEG ILDGVMTGAI ALYDLKVQKN SRTGSVYIVK PKMHGPQEVA 400
    FANKLFTRIE TMLGMAPNTL KMGIMDEERR TSLNLRSCIA QARNRVAFIN 450
    TGFLDRTGDE MHSVMEAGPM LRKNQMKSTP WIKAYERNNV LSGLFCGLRG 500
    KAQIGKGMWA MPDLMADMYS QKGDQLRAGA NTAWVPSPTA ATLHALHYHQ 550
    TNVQSVQANI AQTEFNAEFE PLLDDLLTIP VAENANWSAQ EIQQELDNNV 600
    QGILGYVVRW VEQGIGCSKV PDIHNVALME DRATLRISSQ HIANWLRHGI 650
    LTKEQVQASL ENMAKVVDQQ NAGDPAYRPM AGNFANSCAF KAASDLIFLG 700
    VKQPNGYTEP LLHAWRLREK ESH 723
    Length:723
    Mass (Da):80,489
    Last modified:January 23, 2007 - v3
    Checksum:i820F177D3FE02632
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74547 Genomic DNA. Translation: CAA52639.1.
    U28377 Genomic DNA. Translation: AAA69143.1.
    U00096 Genomic DNA. Translation: AAC76012.1.
    AP009048 Genomic DNA. Translation: BAE77036.1.
    PIRiS51788.
    RefSeqiNP_417450.1. NC_000913.3.
    YP_491172.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76012; AAC76012; b2976.
    BAE77036; BAE77036; BAE77036.
    GeneIDi12930245.
    948857.
    KEGGiecj:Y75_p2904.
    eco:b2976.
    PATRICi32121366. VBIEscCol129921_3070.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74547 Genomic DNA. Translation: CAA52639.1 .
    U28377 Genomic DNA. Translation: AAA69143.1 .
    U00096 Genomic DNA. Translation: AAC76012.1 .
    AP009048 Genomic DNA. Translation: BAE77036.1 .
    PIRi S51788.
    RefSeqi NP_417450.1. NC_000913.3.
    YP_491172.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D8C X-ray 2.00 A 1-723 [» ]
    1P7T X-ray 1.95 A/B 3-723 [» ]
    1Y8B NMR - A 1-723 [» ]
    2JQX NMR - A 1-723 [» ]
    ProteinModelPortali P37330.
    SMRi P37330. Positions 1-723.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9761N.
    IntActi P37330. 6 interactions.
    MINTi MINT-1248166.
    STRINGi 511145.b2976.

    Proteomic databases

    PaxDbi P37330.
    PRIDEi P37330.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76012 ; AAC76012 ; b2976 .
    BAE77036 ; BAE77036 ; BAE77036 .
    GeneIDi 12930245.
    948857.
    KEGGi ecj:Y75_p2904.
    eco:b2976.
    PATRICi 32121366. VBIEscCol129921_3070.

    Organism-specific databases

    EchoBASEi EB4141.
    EcoGenei EG20080. glcB.

    Phylogenomic databases

    eggNOGi COG2225.
    HOGENOMi HOG000220740.
    KOi K01638.
    OMAi PANTLKM.
    OrthoDBi EOG6HJ286.
    PhylomeDBi P37330.

    Enzyme and pathway databases

    UniPathwayi UPA00703 ; UER00720 .
    BioCyci EcoCyc:MALSYNG-MONOMER.
    ECOL316407:JW2943-MONOMER.
    MetaCyc:MALSYNG-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P37330.
    PROi P37330.

    Gene expression databases

    Genevestigatori P37330.

    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. "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, FUNCTION, SUBUNIT, INDUCTION, NOMENCLATURE.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. 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. "Regulation of glyoxylate metabolism in Escherichia coli K-12."
      Ornston L.N., Ornston M.K.
      J. Bacteriol. 98:1098-1108(1969) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION.
    5. "Demonstration of 2 malate synthases in Escherichia coli."
      Falmagne P., Vanderwinkel E., Wiame J.M.
      Biochim. Biophys. Acta 99:246-258(1965) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Cross-induction of glc and ace operons of Escherichia coli attributable to pathway intersection. Characterization of the glc promoter."
      Pellicer M.T., Fernandez C., Badia J., Aguilar J., Lin E.C., Baldom L.
      J. Biol. Chem. 274:1745-1752(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    7. "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) IN COMPLEX WITH SUBSTRATE AND MAGNESIUM ION, ACTIVE SITE, COFACTOR, REACTION MECHANISM, SUBUNIT.
    8. "Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 A resolution."
      Anstrom D.M., Kallio K., Remington S.J.
      Protein Sci. 12:1822-1832(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 3-722 IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM ION, OXIDATION AT CYS-617 AND CYS-688, MUTAGENESIS OF ARG-338; CYS-617 AND ASP-631, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES.
    9. "Solution NMR-derived global fold of a monomeric 82-kDa enzyme."
      Tugarinov V., Choy W.Y., Orekhov V.Y., Kay L.E.
      Proc. Natl. Acad. Sci. U.S.A. 102:622-627(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 3-722, SUBUNIT.
    10. "Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints."
      Grishaev A., Tugarinov V., Kay L.E., Trewhella J., Bax A.
      J. Biomol. NMR 40:95-106(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 3-723.

    Entry informationi

    Entry nameiMASZ_ECOLI
    AccessioniPrimary (citable) accession number: P37330
    Secondary accession number(s): Q2M9M0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 131 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3