ID   B2JST5_PARP8            Unreviewed;       726 AA.
AC   B2JST5;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   04-NOV-2026, entry version 112.
DE   RecName: Full=Malate synthase G {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|NCBIfam:TIGR01345};
DE            EC=2.3.3.9 {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|NCBIfam:TIGR01345};
GN   Name=glcB {ECO:0000256|HAMAP-Rule:MF_00641};
GN   OrderedLocusNames=Bphy_6610 {ECO:0000313|EMBL:ACC75638.1};
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OG   Plasmid pBPHY01 {ECO:0000313|EMBL:ACC75638.1,
OG   ECO:0000313|Proteomes:UP000001192}.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC75638.1, ECO:0000313|Proteomes:UP000001192};
RN   [1] {ECO:0000313|Proteomes:UP000001192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC   {ECO:0000313|Proteomes:UP000001192};
RC   PLASMID=Plasmid pBPHY01 {ECO:0000313|Proteomes:UP000001192};
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA   James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA   Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA   Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT   range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
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.
CC       {ECO:0000256|ARBA:ARBA00054368, ECO:0000256|HAMAP-Rule:MF_00641}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glyoxylate + acetyl-CoA + 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:0000256|HAMAP-
CC         Rule:MF_00641, ECO:0000256|RuleBase:RU003572};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP-
CC         Rule:MF_00641};
CC   -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC       isocitrate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00641,
CC       ECO:0000256|RuleBase:RU003572}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00641}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00641,
CC       ECO:0000256|RuleBase:RU003572}.
CC   -!- SIMILARITY: Belongs to the malate synthase family. GlcB subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00641}.
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DR   EMBL; CP001045; ACC75638.1; -; Genomic_DNA.
DR   RefSeq; WP_012405797.1; NC_010625.1.
DR   AlphaFoldDB; B2JST5; -.
DR   KEGG; bph:Bphy_6610; -.
DR   HOGENOM; CLU_028446_1_0_4; -.
DR   OMA; ADRQYVG; -.
DR   OrthoDB; 9762054at2; -.
DR   UniPathway; UPA00703; UER00720.
DR   Proteomes; UP000001192; Plasmid pBPHY01.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:TreeGrafter.
DR   GO; GO:0004474; F:malate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009436; P:glyoxylate catabolic process; IEA:TreeGrafter.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd00728; malate_synt_G; 1.
DR   FunFam; 3.20.20.360:FF:000002; Malate synthase G; 1.
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   NCBIfam; NF002825; PRK02999.1; 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   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:ACC75638.1};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00641};
KW   Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435, ECO:0000256|HAMAP-
KW   Rule:MF_00641};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00641};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00641};
KW   Oxidation {ECO:0000256|ARBA:ARBA00023097, ECO:0000256|HAMAP-Rule:MF_00641};
KW   Plasmid {ECO:0000313|EMBL:ACC75638.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001192};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00641};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW   Rule:MF_00641}.
FT   DOMAIN          16..76
FT                   /note="Malate synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20656"
FT   DOMAIN          160..234
FT                   /note="Malate synthase G alpha-beta insertion"
FT                   /evidence="ECO:0000259|Pfam:PF20658"
FT   DOMAIN          336..568
FT                   /note="Malate synthase TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01274"
FT   DOMAIN          592..686
FT                   /note="Malate synthase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20659"
FT   ACT_SITE        339
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00641,
FT                   ECO:0000256|PIRSR:PIRSR601465-50"
FT   ACT_SITE        632
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00641,
FT                   ECO:0000256|PIRSR:PIRSR601465-50"
FT   BINDING         118
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT   BINDING         125..126
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT   BINDING         275
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT   BINDING         312
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT   BINDING         339
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT   BINDING         428
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT   BINDING         428
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT   BINDING         453..456
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT   BINDING         456
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT   BINDING         537
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT   MOD_RES         618
FT                   /note="Cysteine sulfenic acid (-SOH)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
SQ   SEQUENCE   726 AA;  79282 MW;  32E3AB6C249820DE CRC64;
     MTQMTQRGGL QVAANLEQFI EKEALPGTGV DSAAFWAGFD AIVHDLAPKN RALLAERDRL
     QVELDTWHRA NPGPVRDLRA YRGFLESIGY IVPTPASVKA TTDNVDSEIA EQAGPQLVVP
     LSNQRYALNA ANARWGSLYD ALYGTDAIDE TDGAERTAKF NPVRGARVIA FARKFLDDAA
     PLENGSHKDS TGYRVENGKL SVALKSGATA LRDPAQFVGY QGDANAPSAV LLKHNGLHFE
     IQIDADDSIG KTDPANIKDV LMEAAVSTII DCEDSVAAVD ADDKVQLYRN WLGLMVGNLT
     EEVTKGGKTF TRRLNADREY HGADGKPVKL HGRSLLFIRN VGHLMTNPAV LDRDGNEIPE
     GILDGVVTTL CALHDRTHKL NSRTGSIYIV KPKMHGPAEV AFASELFARV EDLLGLARNT
     IKMGIMDEER RTSVNLAACI AEAAQRVAFI NTGFLDRTGD EMHSSMEAGP MMRKGDMKSS
     KWIAAYERSN VLVGLAAGLR GRAQIGKGMW AMPDLMKAML EQKIGHPKAG ANTAWVPSPT
     AATLHALHYH QVDVQAVQKE LERTDLASVR DELLDGLLTI PVVEKAQWSD TEIRQEIENN
     AQGILGYVVR WIDQGVGCSK VPDIHNVGLM EDRATLRISS QHIANWLRHG VVRQELVLET
     LKLMAKVVDQ QNAGDPGYKP MAPDFDRSIA FKAACALVFE GCAQPSGYTE PLLHKFRLQL
     KEAGNA
//