MASZ_VARPS
ID MASZ_VARPS Reviewed; 724 AA.
AC C5CJB5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=Vapar_0452;
OS Variovorax paradoxus (strain S110).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=543728;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S110;
RX PubMed=21183664; DOI=10.1128/jb.00925-10;
RA Han J.I., Choi H.K., Lee S.W., Orwin P.M., Kim J., Laroe S.L., Kim T.G.,
RA O'Neil J., Leadbetter J.R., Lee S.Y., Hur C.G., Spain J.C.,
RA Ovchinnikova G., Goodwin L., Han C.;
RT "Complete genome sequence of the metabolically versatile plant growth-
RT promoting endophyte, Variovorax paradoxus S110.";
RL J. Bacteriol. 193:1183-1190(2011).
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; CP001635; ACS17115.1; -; Genomic_DNA.
DR RefSeq; WP_012745615.1; NC_012791.1.
DR AlphaFoldDB; C5CJB5; -.
DR SMR; C5CJB5; -.
DR STRING; 543728.Vapar_0452; -.
DR EnsemblBacteria; ACS17115; ACS17115; Vapar_0452.
DR GeneID; 45054782; -.
DR KEGG; vap:Vapar_0452; -.
DR eggNOG; COG2225; Bacteria.
DR HOGENOM; CLU_028446_1_0_4; -.
DR OMA; MAPGFDG; -.
DR OrthoDB; 322024at2; -.
DR UniPathway; UPA00703; UER00720.
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 3: Inferred from homology;
KW Cytoplasm; Glyoxylate bypass; Magnesium; Metal-binding; Oxidation;
KW Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..724
FT /note="Malate synthase G"
FT /id="PRO_1000212378"
FT ACT_SITE 339
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT ACT_SITE 632
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 118
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 125..126
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 428
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 428
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 453..456
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 456
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 537
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT MOD_RES 618
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
SQ SEQUENCE 724 AA; 77864 MW; 4CE67206D0446EFE CRC64;
MTARTTTHGL QVATELHRFI EDKVLPASGV ASDVFWKGFD AIVHDLAPKN IALLAERDRL
QAELDAWHKK NPGPIADMPA YRAFLEKIGY LLPQPKGAKA TTANVDSELA LQAGPQLVVP
ILNARYALNA ANARWGSLYD ALYGTDAIPE TGGAEKGKGY NPVRGAKVIE FARNVLDQAA
PLENGSHKMA TGYSVKDGKL VVALQSSSTG LADPAQFVGY QGDAAAPSSV LLKHNGIHLD
IRIDRSTPIG KGDAAGVSDL VLEAALSTIL DLEDSVAVVD AADKVVAYSN WLGIVEGTLT
EEVAKGGKTF TRGLNPDREY TGADGRPVKL HGRSLMFLRN VGHLMTNPAV LYAGGKEIPE
GILDAVVTTT IAMIDLKRKG NSRTGSIYIV KPKMHGPAEV AFASELFGRV EQLLGLPANT
VKLGIMDEER RTSVNLKACI AEAAARVAFI NTGFLDRTGD EMHTAMHGGP MIRKGDMKSS
AWIGAYEKNN VLVGLSCGLR GKAQIGKGMW AMPDLMAAML EQKIAHPKAG ANTAWVPSPT
AATLHALHYH QVSVTAVQQE LEKIDADAER DNILNALLQV PIAPAANWTE AEKQQEIDNN
VQGILGYVVR WIDQGVGCSK VPDIHNVGLM EDRATLRISS QHIANWLLHG VVTKAQVDET
FQRMAKVVDE QNAGDPVYQP MAGHFDTSAA YKAAQDLVFK GIEQPSGYTE PLLHAWRLKV
KGEV
