MASZ_ECOLI
ID MASZ_ECOLI Reviewed; 723 AA.
AC P37330; Q2M9M0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Malate synthase G {ECO:0000255|HAMAP-Rule:MF_00641};
DE Short=MSG;
DE EC=2.3.3.9 {ECO:0000255|HAMAP-Rule:MF_00641};
GN Name=glcB {ECO:0000255|HAMAP-Rule:MF_00641}; Synonyms=glc;
GN OrderedLocusNames=b2976, JW2943;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13, FUNCTION,
RP SUBUNIT, INDUCTION, AND NOMENCLATURE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7925370; DOI=10.1111/j.1432-1033.1994.00541.x;
RA Molina I., Badia J., Aguilar J.T., Pellicer M.T., Baldoma L.;
RT "Molecular characterization of Escherichia coli malate synthase G.
RT Differentiation with the malate synthase A isoenzyme.";
RL Eur. J. Biochem. 224:541-548(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=4892366; DOI=10.1128/jb.98.3.1098-1108.1969;
RA Ornston L.N., Ornston M.K.;
RT "Regulation of glyoxylate metabolism in Escherichia coli K-12.";
RL J. Bacteriol. 98:1098-1108(1969).
RN [5]
RP FUNCTION.
RX PubMed=14336062;
RA Falmagne P., Vanderwinkel E., Wiame J.M.;
RT "Demonstration of 2 malate synthases in Escherichia coli.";
RL Biochim. Biophys. Acta 99:246-258(1965).
RN [6]
RP INDUCTION.
RC STRAIN=K12 / MC4100;
RX PubMed=9880556; DOI=10.1074/jbc.274.3.1745;
RA Pellicer M.T., Fernandez C., Badia J., Aguilar J., Lin E.C., Baldom L.;
RT "Cross-induction of glc and ace operons of Escherichia coli attributable to
RT pathway intersection. Characterization of the glc promoter.";
RL J. Biol. Chem. 274:1745-1752(1999).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND
RP MAGNESIUM ION, ACTIVE SITE, COFACTOR, REACTION MECHANISM, AND SUBUNIT.
RX PubMed=10715138; DOI=10.1021/bi992519h;
RA Howard B.R., Endrizzi J.A., Remington S.J.;
RT "Crystal structure of Escherichia coli malate synthase G complexed with
RT magnesium and glyoxylate at 2.0-A resolution: mechanistic implications.";
RL Biochemistry 39:3156-3168(2000).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 3-722 IN COMPLEX WITH SUBSTRATE
RP ANALOGS AND MAGNESIUM ION, OXIDATION AT CYS-617 AND CYS-688, MUTAGENESIS OF
RP ARG-338; CYS-617 AND ASP-631, ACTIVE SITE, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=12930982; DOI=10.1110/ps.03174303;
RA Anstrom D.M., Kallio K., Remington S.J.;
RT "Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-
RT coenzyme A abortive ternary complex at 1.95 A resolution.";
RL Protein Sci. 12:1822-1832(2003).
RN [9]
RP STRUCTURE BY NMR OF 3-722, AND SUBUNIT.
RX PubMed=15637152; DOI=10.1073/pnas.0407792102;
RA Tugarinov V., Choy W.Y., Orekhov V.Y., Kay L.E.;
RT "Solution NMR-derived global fold of a monomeric 82-kDa enzyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:622-627(2005).
RN [10]
RP STRUCTURE BY NMR OF 3-723.
RX PubMed=18008171; DOI=10.1007/s10858-007-9211-5;
RA Grishaev A., Tugarinov V., Kay L.E., Trewhella J., Bax A.;
RT "Refined solution structure of the 82-kDa enzyme malate synthase G from
RT joint NMR and synchrotron SAXS restraints.";
RL J. Biomol. NMR 40:95-106(2008).
CC -!- FUNCTION: Involved in the glycolate utilization. Catalyzes the
CC condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-
CC CoA) and glyoxylate to form malate and CoA. {ECO:0000255|HAMAP-
CC Rule:MF_00641, ECO:0000269|PubMed:14336062, ECO:0000269|PubMed:4892366,
CC ECO:0000269|PubMed:7925370}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+);
CC Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.3.9; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00641};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00641,
CC ECO:0000269|PubMed:10715138};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9 uM for acetyl-CoA (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:12930982};
CC KM=21 uM for glyoxylate (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:12930982};
CC Vmax=36.1 umol/min/mg enzyme (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:12930982};
CC Note=kcat is 48.1 sec(-1) for glyoxylate (at pH 8 and 37 degrees
CC Celsius).;
CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_00641}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00641,
CC ECO:0000269|PubMed:10715138, ECO:0000269|PubMed:12930982,
CC ECO:0000269|PubMed:15637152, ECO:0000269|PubMed:7925370}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By glycolate. Part of the glcDEFGB operon, which is induced
CC by growth on glycolate, under the positive control of GlcC. Also
CC induced by growth on acetate. Expression of the glc operon is strongly
CC dependent on the integration host factor (IHF) and is repressed by the
CC global respiratory regulator ArcA-P (PubMed:9880556).
CC {ECO:0000269|PubMed:4892366, ECO:0000269|PubMed:7925370,
CC ECO:0000269|PubMed:9880556}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to oxidize
CC glyoxylate. {ECO:0000269|PubMed:4892366}.
CC -!- SIMILARITY: Belongs to the malate synthase family. GlcB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00641}.
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DR EMBL; X74547; CAA52639.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69143.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76012.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77036.1; -; Genomic_DNA.
DR PIR; S51788; S51788.
DR RefSeq; NP_417450.1; NC_000913.3.
DR RefSeq; WP_000084131.1; NZ_SSUV01000003.1.
DR PDB; 1D8C; X-ray; 2.00 A; A=1-723.
DR PDB; 1P7T; X-ray; 1.95 A; A/B=3-723.
DR PDB; 1Y8B; NMR; -; A=1-723.
DR PDB; 2JQX; NMR; -; A=1-723.
DR PDBsum; 1D8C; -.
DR PDBsum; 1P7T; -.
DR PDBsum; 1Y8B; -.
DR PDBsum; 2JQX; -.
DR AlphaFoldDB; P37330; -.
DR BMRB; P37330; -.
DR SMR; P37330; -.
DR BioGRID; 4259239; 20.
DR DIP; DIP-9761N; -.
DR IntAct; P37330; 6.
DR MINT; P37330; -.
DR STRING; 511145.b2976; -.
DR DrugBank; DB04343; Glyoxylic acid.
DR jPOST; P37330; -.
DR PaxDb; P37330; -.
DR PRIDE; P37330; -.
DR EnsemblBacteria; AAC76012; AAC76012; b2976.
DR EnsemblBacteria; BAE77036; BAE77036; BAE77036.
DR GeneID; 948857; -.
DR KEGG; ecj:JW2943; -.
DR KEGG; eco:b2976; -.
DR PATRIC; fig|1411691.4.peg.3755; -.
DR EchoBASE; EB4141; -.
DR eggNOG; COG2225; Bacteria.
DR HOGENOM; CLU_028446_1_0_6; -.
DR InParanoid; P37330; -.
DR OMA; FWRNVDE; -.
DR PhylomeDB; P37330; -.
DR BioCyc; EcoCyc:MALSYNG-MON; -.
DR BioCyc; MetaCyc:MALSYNG-MON; -.
DR BRENDA; 2.3.3.9; 2026.
DR UniPathway; UPA00703; UER00720.
DR EvolutionaryTrace; P37330; -.
DR PRO; PR:P37330; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0004474; F:malate synthase activity; IDA:EcoCyc.
DR GO; GO:0009436; P:glyoxylate catabolic process; IEP:EcoCyc.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd00728; malate_synt_G; 1.
DR DisProt; DP01837; -.
DR Gene3D; 1.20.1220.12; -; 1.
DR Gene3D; 3.20.20.360; -; 2.
DR HAMAP; MF_00641; Malate_synth_G; 1.
DR InterPro; IPR044856; Malate_synth_C_sf.
DR InterPro; IPR011076; Malate_synth_sf.
DR InterPro; IPR001465; Malate_synthase.
DR InterPro; IPR006253; Malate_synthG.
DR InterPro; IPR046363; MS_N_TIM-barrel_dom.
DR PANTHER; PTHR42739; PTHR42739; 1.
DR Pfam; PF01274; Malate_synthase; 1.
DR SUPFAM; SSF51645; SSF51645; 1.
DR TIGRFAMs; TIGR01345; malate_syn_G; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Glyoxylate bypass;
KW Magnesium; Metal-binding; Oxidation; Reference proteome; Transferase;
KW Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7925370"
FT CHAIN 2..723
FT /note="Malate synthase G"
FT /id="PRO_0000166886"
FT ACT_SITE 338
FT /note="Proton acceptor"
FT ACT_SITE 631
FT /note="Proton donor"
FT BINDING 118
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT BINDING 125..126
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT BINDING 274
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT BINDING 311
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT BINDING 338
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT BINDING 427
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT BINDING 427
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 452..455
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 536
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT MOD_RES 617
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641,
FT ECO:0000269|PubMed:12930982"
FT MOD_RES 688
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641,
FT ECO:0000269|PubMed:12930982"
FT MUTAGEN 338
FT /note="R->K: Has a specific activity which is only 6.6% of
FT the wild-type activity."
FT /evidence="ECO:0000269|PubMed:12930982"
FT MUTAGEN 617
FT /note="C->S: Affinity binding for acetyl-CoA is more than
FT five times greater than that of wild-type, although its
FT specific activity is comparable."
FT /evidence="ECO:0000269|PubMed:12930982"
FT MUTAGEN 631
FT /note="D->N: Absence of malate synthase activity."
FT /evidence="ECO:0000269|PubMed:12930982"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 32..70
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1Y8B"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 138..143
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:1D8C"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:2JQX"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1D8C"
FT HELIX 160..177
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 265..272
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 280..294
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:1P7T"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:1Y8B"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:1Y8B"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 359..377
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 396..412
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 420..426
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 429..432
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 435..440
FT /evidence="ECO:0007829|PDB:1P7T"
FT TURN 441..445
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 446..451
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 453..463
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 480..495
FT /evidence="ECO:0007829|PDB:1P7T"
FT TURN 499..501
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 502..506
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 515..521
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 523..527
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 531..537
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 538..550
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 553..560
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 565..576
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 589..613
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 618..621
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 627..630
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 632..647
FT /evidence="ECO:0007829|PDB:1P7T"
FT TURN 648..650
FT /evidence="ECO:0007829|PDB:2JQX"
FT HELIX 653..670
FT /evidence="ECO:0007829|PDB:1P7T"
FT TURN 671..673
FT /evidence="ECO:0007829|PDB:1P7T"
FT STRAND 674..676
FT /evidence="ECO:0007829|PDB:2JQX"
FT TURN 680..683
FT /evidence="ECO:0007829|PDB:2JQX"
FT HELIX 684..686
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 688..698
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 700..702
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 704..706
FT /evidence="ECO:0007829|PDB:1P7T"
FT HELIX 709..720
FT /evidence="ECO:0007829|PDB:1P7T"
SQ SEQUENCE 723 AA; 80489 MW; 820F177D3FE02632 CRC64;
MSQTITQSRL RIDANFKRFV DEEVLPGTGL DAAAFWRNFD EIVHDLAPEN RQLLAERDRI
QAALDEWHRS NPGPVKDKAA YKSFLRELGY LVPQPERVTV ETTGIDSEIT SQAGPQLVVP
AMNARYALNA ANARWGSLYD ALYGSDIIPQ EGAMVSGYDP QRGEQVIAWV RRFLDESLPL
ENGSYQDVVA FKVVDKQLRI QLKNGKETTL RTPAQFVGYR GDAAAPTCIL LKNNGLHIEL
QIDANGRIGK DDPAHINDVI VEAAISTILD CEDSVAAVDA EDKILLYRNL LGLMQGTLQE
KMEKNGRQIV RKLNDDRHYT AADGSEISLH GRSLLFIRNV GHLMTIPVIW DSEGNEIPEG
ILDGVMTGAI ALYDLKVQKN SRTGSVYIVK PKMHGPQEVA FANKLFTRIE TMLGMAPNTL
KMGIMDEERR TSLNLRSCIA QARNRVAFIN TGFLDRTGDE MHSVMEAGPM LRKNQMKSTP
WIKAYERNNV LSGLFCGLRG KAQIGKGMWA MPDLMADMYS QKGDQLRAGA NTAWVPSPTA
ATLHALHYHQ TNVQSVQANI AQTEFNAEFE PLLDDLLTIP VAENANWSAQ EIQQELDNNV
QGILGYVVRW VEQGIGCSKV PDIHNVALME DRATLRISSQ HIANWLRHGI LTKEQVQASL
ENMAKVVDQQ NAGDPAYRPM AGNFANSCAF KAASDLIFLG VKQPNGYTEP LLHAWRLREK
ESH
