ID A0A0Q5NQJ4_9BURK Unreviewed; 725 AA.
AC A0A0Q5NQJ4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Malate synthase G {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572};
DE EC=2.3.3.9 {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572};
GN Name=glcB {ECO:0000256|HAMAP-Rule:MF_00641};
GN ORFNames=ASG35_18055 {ECO:0000313|EMBL:KQR74647.1};
OS Burkholderia sp. Leaf177.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1736287 {ECO:0000313|EMBL:KQR74647.1, ECO:0000313|Proteomes:UP000051826};
RN [1] {ECO:0000313|EMBL:KQR74647.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR74647.1,
RC ECO:0000313|Proteomes:UP000051826};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR74647.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR74647.1,
RC ECO:0000313|Proteomes:UP000051826};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00001699, 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,
CC ECO:0000256|HAMAP-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQR74647.1}.
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DR EMBL; LMPF01000024; KQR74647.1; -; Genomic_DNA.
DR RefSeq; WP_056364297.1; NZ_LMPF01000024.1.
DR AlphaFoldDB; A0A0Q5NQJ4; -.
DR OrthoDB; 9762054at2; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000051826; Unassembled WGS sequence.
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; 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 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:KQR74647.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000051826};
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 19..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..578
FT /note="Malate synthase TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01274"
FT DOMAIN 592..687
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 725 AA; 78924 MW; 38E1B13DF773E42B CRC64;
MSQMIKRNGL QVADVLAKYV DDEALSGVGI ESEAFWKGFD ALVHDLAPKN RALLAERDRL
QVELDQWHKA NPGPVRDLKA YRGFLESIGY IVPSSAVVKA TTQNVDTEIA TQAGPQLVVP
LSNQRYALNA ANARWGSLYD ALYGTDAIPD THGGERTAQF NPARGAAVIA RARAFLDEAA
PLANGSHADA TAYRVEGGKL TVALKSGSSA LKFPEQFIGF QGDANAPSAI LLKHNGLHFE
IQIDATDSIG KTDSAHVKDV LMEAAVSTII DCEDSVAAVD AADKVQLYRN WTGLMKGDLA
EDVTKNGKTF TRRLNADREY TAPDGSSVKL HGRSLLFIRN VGHLMTNPSV IDRDGHEIPE
GILDAVMTSL GAVHDLKNKL NSRTGSIYIV KPKMHGPAEV AFSDELFGRV EDLLGLPRHT
IKIGIMDEER RTSVNLQACI AAASARVAFI NTGFLDRTGD EMHSAMEAGP MMRKGDMKSS
AWITAYERNN VLAGLSSGLR GRAQIGKGMW AMPDLMHAML EQKIAHPKAG ANTAWVPSPT
AATLHALHYH QVDVQAVQQE LEKTGYDSAR DALLDGLLTI PVVEKADWSD AEIRQEIENN
AQGILGYVVR WVDQGVGCSK VPDIHDIGLM EDRATLRISS QHIANWLYHG VVSEALVNET
FERMAKVVDA QNANDPHYQP MAGHFETSLA FKAAKALVFE GRAQPSGYTE PLLHKFRLEV
KALRG
//
