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 27-MAR-2024, entry version 192. 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; Pseudomonadota; 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00641, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7YQM; EM; 2.89 A; A=1-723. DR PDB; 7YQN; X-ray; 1.60 A; A/B=1-723. DR PDBsum; 1D8C; -. DR PDBsum; 1P7T; -. DR PDBsum; 1Y8B; -. DR PDBsum; 2JQX; -. DR PDBsum; 7YQM; -. DR PDBsum; 7YQN; -. 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; 511145-b2976; -. DR EnsemblBacteria; AAC76012; AAC76012; b2976. 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; QEIDNNC; -. DR OrthoDB; 9762054at2; -. DR PhylomeDB; P37330; -. DR BioCyc; EcoCyc:MALSYNG-MONOMER; -. DR BioCyc; MetaCyc:MALSYNG-MONOMER; -. 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; 3.20.20.360; Malate synthase, domain 3; 2. DR Gene3D; 1.20.1220.12; Malate synthase, domain III; 1. 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_TIM. DR InterPro; IPR006253; Malate_synthG. DR InterPro; IPR048355; MS_C. DR InterPro; IPR048356; MS_N. DR InterPro; IPR046363; MS_N_TIM-barrel_dom. DR InterPro; IPR048357; MSG_insertion. DR NCBIfam; TIGR01345; malate_syn_G; 1. DR PANTHER; PTHR42739; MALATE SYNTHASE G; 1. DR PANTHER; PTHR42739:SF1; MALATE SYNTHASE G; 1. DR Pfam; PF20659; MS_C; 1. DR Pfam; PF20656; MS_N; 1. DR Pfam; PF01274; MS_TIM-barrel; 1. DR Pfam; PF20658; MSG_insertion; 1. DR SUPFAM; SSF51645; Malate synthase 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 4..7 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 10..13 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 14..23 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 26..28 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 32..70 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:1Y8B" FT HELIX 78..87 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 107..110 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 114..120 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 124..131 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 132..134 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 135..137 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 138..143 FT /evidence="ECO:0007829|PDB:7YQN" 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:7YQN" FT STRAND 180..183 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 185..187 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 188..194 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 197..202 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 213..215 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 216..222 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 225..233 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 236..242 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 249..251 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 256..262 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 266..272 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 280..294 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 299..301 FT /evidence="ECO:0007829|PDB:7YQN" FT TURN 303..305 FT /evidence="ECO:0007829|PDB:7YQM" FT STRAND 306..309 FT /evidence="ECO:0007829|PDB:7YQM" FT STRAND 310..312 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 317..321 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 326..329 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 331..333 FT /evidence="ECO:0007829|PDB:1Y8B" FT STRAND 334..338 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 345..350 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 356..358 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 359..377 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 382..384 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 386..390 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 396..413 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 420..425 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 429..432 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 435..440 FT /evidence="ECO:0007829|PDB:7YQN" FT TURN 441..445 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 446..450 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 454..463 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 465..467 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 473..478 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 480..495 FT /evidence="ECO:0007829|PDB:7YQN" FT TURN 499..501 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 502..506 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 515..521 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 523..527 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 531..537 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 538..550 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 553..560 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 565..568 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 569..576 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 589..613 FT /evidence="ECO:0007829|PDB:7YQN" FT STRAND 618..621 FT /evidence="ECO:0007829|PDB:1P7T" FT STRAND 627..630 FT /evidence="ECO:0007829|PDB:1P7T" FT HELIX 633..647 FT /evidence="ECO:0007829|PDB:7YQN" FT TURN 648..650 FT /evidence="ECO:0007829|PDB:2JQX" FT HELIX 653..670 FT /evidence="ECO:0007829|PDB:7YQN" FT TURN 671..673 FT /evidence="ECO:0007829|PDB:7YQN" 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:7YQN" FT HELIX 688..698 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 700..702 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 704..706 FT /evidence="ECO:0007829|PDB:7YQN" FT HELIX 709..720 FT /evidence="ECO:0007829|PDB:7YQN" 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 //