MASZ_BRUA4
ID MASZ_BRUA4 Reviewed; 728 AA.
AC A6WYD2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=Oant_1269;
OS Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=439375;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC 15819 / NCTC 12168 / Alc 37;
RX PubMed=21685287; DOI=10.1128/jb.05335-11;
RA Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA Ugalde R.A., Garcia E., Tolmasky M.E.;
RT "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT pathogen and symbiont of several eukaryotic hosts.";
RL J. Bacteriol. 193:4274-4275(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; CP000758; ABS13986.1; -; Genomic_DNA.
DR RefSeq; WP_012091375.1; NC_009667.1.
DR AlphaFoldDB; A6WYD2; -.
DR SMR; A6WYD2; -.
DR STRING; 439375.Oant_1269; -.
DR EnsemblBacteria; ABS13986; ABS13986; Oant_1269.
DR KEGG; oan:Oant_1269; -.
DR PATRIC; fig|439375.7.peg.1330; -.
DR eggNOG; COG2225; Bacteria.
DR HOGENOM; CLU_028446_1_0_5; -.
DR OMA; MAPGFDG; -.
DR OrthoDB; 322024at2; -.
DR PhylomeDB; A6WYD2; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000002301; Chromosome 1.
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 Reference proteome; Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..728
FT /note="Malate synthase G"
FT /id="PRO_1000056916"
FT ACT_SITE 345
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT ACT_SITE 636
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 123
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 130..131
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 281
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 318
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 345
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 437
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 437
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 462..465
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 546
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT MOD_RES 622
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
SQ SEQUENCE 728 AA; 79664 MW; 89C758B66592CB10 CRC64;
MVSQKAGNYV EIEGLRVAPE LVEFLAKEAA PGTGVEPEKF WKGFAAIIRD LAPKNRALLA
KRDDLQAKID AWYKQNRDKG YSQADYQQFL KNIGYLLPEG GEFSVSTTNV DPEITHIAGP
QLVVPVMNAR YALNAANARW GSLYDALYGT DAISDADGGE KGKGYNPKRG EKVIAWAKNF
LDESAPLATG NWANVAGLAV KDGKLEIKLT DGSATALKDA NQFKGYNGDA AAPTNVLLAK
NNMHVDIVVN ADHPIGKTDP AHIADVVLES AVSTIQDCED SIAAVDAEDK VAVYRNWLGL
MNGKLEDTFE KNGKQMTRRL NGDRSYKAAD GSTLSLKGRS LMLVRNVGHL MTNPAIIDAD
GHEVPEGIMD AAFTSLIALH DIGPNGRHMN SREGSVYIVK PKMHGPEEVA FANEIFTRTE
EMLGMKPNTL KIGIMDEERR TTVNLKEAIR AAKERVVFIN TGFLDRTGDE IHTSMEAGPM
IRKGDMKQAA WIGAYEQWNV DIGLECGLSG HAQIGKGMWA MPDLMAAMLE QKIAHPKAGA
NTAWVPSPTA ATLHATHYHQ VDVAAVQAKL KSRPRAKLDD ILSVPVATRP NWTPEDIQHE
IDNNAQGILG YVVRWVDQGV GCSKVPDINN VGLMEDRATL RISAQHIANW LYHGVVSEAQ
VMETMKRMAA VVDKQNEGDA LYRPMAADFD KSIAFQAACD LVFKGREQPN GYTEPVLHRR
RLELKAQG
