ID MASZ_BORPD Reviewed; 726 AA. AC A9IHH4; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 94. 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}; GN OrderedLocusNames=Bpet4866; OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=340100; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448; RX PubMed=18826580; DOI=10.1186/1471-2164-9-449; RA Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H., RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V., RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S., RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C., RA Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T., RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O., RA Martinez-Arias R.; RT "The missing link: Bordetella petrii is endowed with both the metabolic RT versatility of environmental bacteria and virulence traits of pathogenic RT Bordetellae."; RL BMC Genomics 9:449-449(2008). 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; Evidence={ECO:0000255|HAMAP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AM902716; CAP45218.1; -; Genomic_DNA. DR AlphaFoldDB; A9IHH4; -. DR SMR; A9IHH4; -. DR STRING; 94624.Bpet4866; -. DR KEGG; bpt:Bpet4866; -. DR eggNOG; COG2225; Bacteria. DR UniPathway; UPA00703; UER00720. DR Proteomes; UP000001225; 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; 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 Cytoplasm; Glyoxylate bypass; Magnesium; Metal-binding; Oxidation; KW Transferase; Tricarboxylic acid cycle. FT CHAIN 1..726 FT /note="Malate synthase G" FT /id="PRO_1000130887" FT ACT_SITE 338 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT ACT_SITE 631 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 274 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 311 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 338 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 427 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 427 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 452..455 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 455 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 536 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT MOD_RES 617 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" SQ SEQUENCE 726 AA; 78962 MW; 9248C75C6A1258C5 CRC64; MTERIQQDGL QVAAVLHRFI QDEALPAGGI DAPRFWAGFA ALVRDLAPRN RALLAERDRL QRELDTWHRA HPGPVRDLRA YRAFLEQIGY LQPVPGTVRV ETANVDAEIA EQAGPQLVVP MSNARYALNA ANARWGSLYD ALYGTDAIPP TPGDTGRGYH PQRGQAVIAR ARAFLDEAVP LAQGSHADAT GYSVDNGQLR VALAQGSTGL AQPEQFAGYQ GDAQAPQAIL LKHHGLHIEI QIDRAHSIGA TDAAGIKDVV VEAALTTIMD CEDSVAAVDA EDKVQVYRNW LGLMKGDLAE QVTKGGQTFT RRLNADRVYH APGGGTLTLH GRSLMFVRNV GHLMTNPAVL DADGNEIPEG ILDAVVTTLA ALPDRASRRN SRAGSIYIVK PKMHGPAEAA FANELFDRVE DLLGLPRHTV KMGIMDEERR TSVNLKACIQ AAAGRVAFIN TGFLDRTGDE MHSSMEAGPM MRKGDMKSSA WIAAYERSNV LVGLDCGLRG RAQIGKGMWA MPDLMAAMLE QKIGHPKAGA NTAWVPSPTA ATLHALHYHQ VDVPAVQQQL ESTRLASVQD ELLDGLLTVP VGNPADWSPD DIRHELENNA QGILGYVVRW IDQGVGCSKV PDINNVGLME DRATLRISSQ HIANWMRHGI ATREQVRDTF ERMAAVVDRQ NAGDPLYQPM AGHFDTSIAF QAACALVFEG LAQPNGYTEP LLHQYRLAFK ARHNKG //