MASZ_CORGL
ID MASZ_CORGL Reviewed; 739 AA.
AC P42450;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Malate synthase G {ECO:0000255|HAMAP-Rule:MF_00641};
DE EC=2.3.3.9 {ECO:0000255|HAMAP-Rule:MF_00641};
GN Name=glcB {ECO:0000255|HAMAP-Rule:MF_00641}; Synonyms=aceB;
GN OrderedLocusNames=Cgl2329, cg2559;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION,
RP CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=7812449; DOI=10.1099/13500872-140-11-3099;
RA Reinscheid D.J., Eikmanns B.J., Sahm H.;
RT "Malate synthase from Corynebacterium glutamicum: sequence analysis of the
RT gene and biochemical characterization of the enzyme.";
RL Microbiology 140:3099-3108(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RA Lee H.S., Sinskey A.J.;
RT "Molecular characterization of aceB, a gene encoding malate synthase in
RT Corynebacterium glutamicum.";
RL J. Microbiol. Biotechnol. 4:256-263(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [5]
RP INDUCTION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=15090522; DOI=10.1128/jb.186.9.2798-2809.2004;
RA Gerstmeir R., Cramer A., Dangel P., Schaffer S., Eikmanns B.J.;
RT "RamB, a novel transcriptional regulator of genes involved in acetate
RT metabolism of Corynebacterium glutamicum.";
RL J. Bacteriol. 186:2798-2809(2004).
RN [6]
RP INDUCTION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=16547043; DOI=10.1128/jb.188.7.2554-2567.2006;
RA Cramer A., Gerstmeir R., Schaffer S., Bott M., Eikmanns B.J.;
RT "Identification of RamA, a novel LuxR-type transcriptional regulator of
RT genes involved in acetate metabolism of Corynebacterium glutamicum.";
RL J. Bacteriol. 188:2554-2567(2006).
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:7812449}.
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, ECO:0000269|PubMed:7812449};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00641,
CC ECO:0000269|PubMed:7812449};
CC Note=Mg(2+). Co(2+) or Mn(2+) could partially replace magnesium.
CC {ECO:0000255|HAMAP-Rule:MF_00641, ECO:0000269|PubMed:7812449};
CC -!- ACTIVITY REGULATION: Inhibited by oxalate, glycolate and ATP.
CC {ECO:0000269|PubMed:7812449}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12 uM for acetyl-CoA (at pH 7.6 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:7812449};
CC KM=30 uM for glyoxylate (at pH 7.6 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:7812449};
CC pH dependence:
CC Optimum pH is 7.6. {ECO:0000269|PubMed:7812449};
CC Temperature dependence:
CC Optimum temperature is 43 degrees Celsius.
CC {ECO:0000269|PubMed:7812449};
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:7812449}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00641,
CC ECO:0000269|PubMed:7812449}.
CC -!- INDUCTION: Activated by RamA and repressed by RamB.
CC {ECO:0000269|PubMed:15090522, ECO:0000269|PubMed:16547043}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show the absence of
CC malate synthase activity and to the inability to grow on acetate.
CC {ECO:0000269|PubMed:7812449}.
CC -!- SIMILARITY: Belongs to the malate synthase family. GlcB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00641}.
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DR EMBL; X78491; CAA55243.1; -; Genomic_DNA.
DR EMBL; L27123; AAA68074.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99722.1; -; Genomic_DNA.
DR EMBL; BX927154; CAF20673.1; -; Genomic_DNA.
DR PIR; I40715; I40715.
DR RefSeq; NP_601530.1; NC_003450.3.
DR RefSeq; WP_011015044.1; NC_006958.1.
DR AlphaFoldDB; P42450; -.
DR SMR; P42450; -.
DR STRING; 196627.cg2559; -.
DR KEGG; cgb:cg2559; -.
DR KEGG; cgl:Cgl2329; -.
DR PATRIC; fig|196627.13.peg.2263; -.
DR eggNOG; COG2225; Bacteria.
DR HOGENOM; CLU_028446_1_0_11; -.
DR OMA; MAPGFDG; -.
DR BRENDA; 2.3.3.9; 960.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004474; F:malate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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 Cytoplasm; Direct protein sequencing; Glyoxylate bypass; Magnesium;
KW Metal-binding; Oxidation; Reference proteome; Transferase;
KW Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7812449"
FT CHAIN 2..739
FT /note="Malate synthase G"
FT /id="PRO_0000166885"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 356
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT ACT_SITE 647
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 135
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 142..143
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 292
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 329
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 356
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 447
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 447
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 472..475
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 475
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 556
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT MOD_RES 633
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
SQ SEQUENCE 739 AA; 82363 MW; DE9AC15F65CCC8EB CRC64;
MTEQELLSAQ TADNAGTDST ERVDAGGMQV AKVLYDFVTE AVLPRVGVDA EKFWSGFAAI
ARDLTPRNRE LLARRDELQM LIDDYHRNNS GTIDQEAYED FLKEIGYLVE EPEAAEIRTQ
NVDTEISSTA GPQLVVPILN ARFALNAANA RWGSLYDALY GTNAIPETDG AEKGKEYNPV
RGQKVIEWGR EFLDSVVPLD GASHADVEKY NITDGKLAAH IGDSVYRLKN RESYRGFTGN
FLDPEAILLE TNGLHIELQI DPVHPIGKAD KTGLKDIVLE SAITTIMDFE DSVAAVDAED
KTLGYSNWFG LNTGELKEEM SKNGRIFTRE LNKDRVYIGR NGTELVLHGR SLLFVRNVGH
LMQNPSILID GEEIFEGIMD AVLTTVCAIP GIAPQNKMRN SRKGSIYIVK PKQHGPEEVA
FTNELFGRVE DLLDLPRHTL KVGVMDEERR TSVNLDASIM EVADRLAFIN TGFLDRTGDE
IHTSMEAGAM VRKADMQTAP WKQAYENNNV DAGIQRGLPG KAQIGKGMWA MTELMAEMLE
KKIGQPREGA NTAWVPSPTG ATLHATHYHL VDVFKVQDEL RAAGRRDSLR NILTIPTAPN
TNWSEEEKKE EMDNNCQSIL GYVVRWVEHG VGCSKVPDIH DIDLMEDRAT LRISSQMLAN
WIRHDVVSKE QVLESLERMA VVVDKQNAGD EAYRDMAPNY DASLAFQAAK DLIFEGTKSP
SGYTEPILHA RRREFKAKN
