GenomeNet

Database: UniProt
Entry: MASZ_CORGL
LinkDB: MASZ_CORGL
Original site: 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   24-JAN-2024, entry version 147.
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; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; 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}.
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; 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; DWNVDIG; -.
DR   OrthoDB; 9762054at2; -.
DR   BioCyc; CORYNE:G18NG-11926-MONOMER; -.
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; 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   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
//
DBGET integrated database retrieval system