MASZ_GEOTN
ID MASZ_GEOTN Reviewed; 727 AA.
AC A4IN50;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=GTNG_1384;
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2;
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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; CP000557; ABO66754.1; -; Genomic_DNA.
DR RefSeq; WP_008879330.1; NC_009328.1.
DR AlphaFoldDB; A4IN50; -.
DR SMR; A4IN50; -.
DR STRING; 420246.GTNG_1384; -.
DR EnsemblBacteria; ABO66754; ABO66754; GTNG_1384.
DR KEGG; gtn:GTNG_1384; -.
DR eggNOG; COG2225; Bacteria.
DR HOGENOM; CLU_028446_1_0_9; -.
DR OMA; MAPGFDG; -.
DR OrthoDB; 322024at2; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000001578; 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 CDD; cd00728; malate_synt_G; 1.
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 Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..727
FT /note="Malate synthase G"
FT /id="PRO_1000056903"
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 275
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 312
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 727 AA; 81200 MW; 37B1B2D489B3ADA2 CRC64;
MIEYVQAGTI QVAKVLYEFV NEELLPNSGL DQDKFWSDFA ALIADLTPRN KELLARRDEI
QEKLNEWYKE HRGRFDFHEY KAFLTDIGYL EPEVEDFEIT TDNVDEEIAV QAGPQLVVPL
TNARYALNAA NARWGSLYDA LYGTDAISEE DGAERGSSYN PVRGAKVIAY GRQFLDEAVP
LVEHSHKDAV QYAIVDGKLV VTTEGGATTG LKEPEKLIGF QGEPQNPTAV LLKNNGLHIE
IQIDREHPVG KTDKAGIKDI VLEAAVTTIM DGEDSVAAVD AEDKVVVYRN LFGLIKGDLT
ATFEKNGKRL TRTLNPDREY KTPDGGELVL PGRSLMFVRN VGHLMTNNAI LDANGEEVYE
GIIDAVVTSL IMKHSLIGNT RYLNSRKGSI YIVKPKMHGS AEVAFANELF DRVEDMLGLE
RNTIKIGVMD EERRTSLNLK NCIYEVRDRI VFINTGFLDR TGDEIHTSME AGPMRRKNDM
KSSTWLAGYE KSNVAVGLAA GFRGRAQIGK GMWAMPDLMA EMLKQKGAQL KAGANTAWVP
SPTAATLHAL HYHQVNVAAV QNELANDRND YRDDILQIPV VDNPQWTADE IQEELDNNCQ
SILGYVVRWI DQGIGCSKVP DIHNIGLMED RATLRISSQI LANWLHHGIC TKEQVLETFK
RMAKVVDEQN AGDPNYRPMA PNYDDSVAFQ AACDLVFLGY EQPNGYTEPI LHRRRQEAKA
KFAAVQQ
