ID MASZ_COREF Reviewed; 748 AA. AC Q8FNB3; DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 124. 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}; Synonyms=masZ; GN OrderedLocusNames=CE2231; OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 OS / NBRC 100395). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196164; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395; RX PubMed=12840036; DOI=10.1101/gr.1285603; RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.; RT "Comparative complete genome sequence analysis of the amino acid RT replacements responsible for the thermostability of Corynebacterium RT efficiens."; RL Genome Res. 13:1572-1579(2003). 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; BA000035; BAC19041.1; -; Genomic_DNA. DR AlphaFoldDB; Q8FNB3; -. DR SMR; Q8FNB3; -. DR STRING; 196164.gene:10742662; -. DR KEGG; cef:CE2231; -. DR eggNOG; COG2225; Bacteria. DR HOGENOM; CLU_028446_1_0_11; -. DR UniPathway; UPA00703; UER00720. DR Proteomes; UP000001409; 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 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 Reference proteome; Transferase; Tricarboxylic acid cycle. FT CHAIN 1..748 FT /note="Malate synthase G" FT /id="PRO_0000166884" FT ACT_SITE 362 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT ACT_SITE 653 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 141 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 148..149 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 298 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 335 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 362 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 453 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 453 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 478..481 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 481 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 562 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT MOD_RES 639 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" SQ SEQUENCE 748 AA; 83491 MW; F9550473EC4E9A09 CRC64; MPAHTRSLAS KELCMNHQQI DAADKTERVT VGGMQVAKVL RDFLTESVLP RVGVDAERFW NGFGDIVRDM TPRNRELLAR RDELQAQLDE YYRENPGKPD PEKYEAFLRE IGYLVDEPAP AEIRTQNIDS EIATTAGPQL VVPILNARFA LNAANARWGS LYDALYGTNA IPDEDGAERG AEYNPVRGQK VIQWGRDFLD AVLPLDGASH ADVEKYNITD GKLAAHVNDG IYRLKDRDAY LGFTGYFEDP TSILLQNNGL HIELQIDPTH PIGKEDKTGL KDIILESAIT TIMDFEDSVA AVDAEDKTLG YRNWFLLNTG ELTEEVAKGD RTFTRKLNDD RVFIGKNGAE LTLHGRSLLF VRNVGHLMTN PAILVDGEEI YEGIMDAIIT TVCAIPGIAP QNKKKNSRKG SIYIVKPKQH GPEEVAFTNE LFARVEDLLD LPRHTLKVGV MDEERRTSVN LDACIMEVAD RLAFINTGFL DRTGDEIHTS MEAGAMVRKA DMQTAPWKQA YEDNNVDAGI QRGLPGKAQI GKGMWAMTEL MGEMLEKKIG QLREGANTAW VPSPTGATLH ATHYHRVDVF KVQDELRAAG RRDSLGKILD VPVAPDTNWT DAEKREELDN NCQSILGYVV RWVEQGVGCS KVPDIHDIDL MEDRATLRIS SQILANWLRH GVVTEEQVIE SLERMAVVVD EQNAGDPNYL NMAPNFTESV AFQAARDLIL KGTESPAGYT EPILHARRRE FKELHGIK //