MASZ_BRADU
ID MASZ_BRADU Reviewed; 721 AA.
AC Q89UE3;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
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}; OrderedLocusNames=bll1474;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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}.
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 -!- 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00641}.
CC -!- SIMILARITY: Belongs to the malate synthase family. GlcB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00641}.
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DR EMBL; BA000040; BAC46739.1; -; Genomic_DNA.
DR RefSeq; NP_768114.1; NC_004463.1.
DR RefSeq; WP_011084290.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89UE3; -.
DR SMR; Q89UE3; -.
DR STRING; 224911.27349726; -.
DR EnsemblBacteria; BAC46739; BAC46739; BAC46739.
DR GeneID; 64021353; -.
DR KEGG; bja:bll1474; -.
DR PATRIC; fig|224911.44.peg.908; -.
DR eggNOG; COG2225; Bacteria.
DR HOGENOM; CLU_028446_1_0_5; -.
DR InParanoid; Q89UE3; -.
DR OMA; MAPGFDG; -.
DR PhylomeDB; Q89UE3; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0004474; F:malate synthase activity; IBA:GO_Central.
DR GO; GO:0009436; P:glyoxylate catabolic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Cytoplasm; Glyoxylate bypass; Magnesium; Metal-binding; Oxidation;
KW Reference proteome; Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..721
FT /note="Malate synthase G"
FT /id="PRO_0000166881"
FT ACT_SITE 339
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT ACT_SITE 630
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 117
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 124..125
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 274
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 311
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 339
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 431
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 431
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 456..459
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 540
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT MOD_RES 616
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
SQ SEQUENCE 721 AA; 77928 MW; B34A9EBCEDA1422E CRC64;
MKRVDAHGLK IAPVLFDFIA KEAAPKTGIA PDAFWAGVAA IIKDLGPKNR ALLALRDALQ
AKIDDWHRAN KGKAFDLNAY TAFLKEIGYL VPEPATQKVE TANVDEEIGK ICGPQLVVPL
TNARYALNAA NARWGSLYDA FYGTDAIPHD PSESGKGYNK ARGDKVIAKA KAFLDAAVPL
ATGSHTDVTA YSIVAGQLAV KLKSGNATAL KNAAQFAGFQ GDAAAPSAVL LVNNGLHVEV
TINRNSAIGK DDPAGVADMV MEAAVSTILD MEDSVAAVDA EDKVLVYRNT LGLMNGTLSA
DFEKGGKTLT RSLNADRSYK TPDGKGEVKL HGRSLLLMRN CGHHMFTDAV LDERGEEVPE
GLLDAAVSGL LAIHDLKGNS KVKNSRTGSA YIVKPKMHGP DEVSFTCEIF DRVEKMLGLP
ENTLKVGIMD EERRTTVNLK ACIQRASKRI MFINTGFLDR TGDEIHTSME AGPMIRKNEM
KAQAWIKAYE DWNVDMGLID GLPGHAQIGK GMWAAPDKMA DMLAQKLAHP QAGATTAWVP
SPTAATLHAL HYHQVNVIAR QEELTKGGPR AKLSDILTIP VSKSNWAPDD VKQEIDNNCQ
GILGYVVRWI DQGVGCSKVP DIHDVGLMED RATLRISSQH LANWLHQGVI TEAQVMESLK
RMAVVVDKQN AGDAIYKPMA PAFDGVAFKA ACDLIFKGRE QPNGYTEYIL TARRREAKAA
G
