ID MASZ_NOCFA Reviewed; 726 AA. AC Q5YWU1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 27-MAR-2024, entry version 113. 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=NFA_25030; OS Nocardia farcinica (strain IFM 10152). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae; OC Nocardia. OX NCBI_TaxID=247156; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IFM 10152; RX PubMed=15466710; DOI=10.1073/pnas.0406410101; RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K., RA Shiba T., Hattori M.; RT "The complete genomic sequence of Nocardia farcinica IFM 10152."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004). 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; AP006618; BAD57350.1; -; Genomic_DNA. DR RefSeq; WP_011209035.1; NC_006361.1. DR AlphaFoldDB; Q5YWU1; -. DR SMR; Q5YWU1; -. DR STRING; 247156.NFA_25030; -. DR GeneID; 61133251; -. DR KEGG; nfa:NFA_25030; -. DR eggNOG; COG2225; Bacteria. DR HOGENOM; CLU_028446_1_0_11; -. DR OrthoDB; 9762054at2; -. DR UniPathway; UPA00703; UER00720. DR Proteomes; UP000006820; 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 Reference proteome; Transferase; Tricarboxylic acid cycle. FT CHAIN 1..726 FT /note="Malate synthase G" FT /id="PRO_1000056915" FT ACT_SITE 340 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT ACT_SITE 632 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 276 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 313 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 340 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 432 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 432 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 457..460 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 460 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 541 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT MOD_RES 618 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" SQ SEQUENCE 726 AA; 79260 MW; 633308E4D3C79077 CRC64; MTERIQVGGL QVAKVLHDFI ENEALPGSGV DSAAFWAGAE QVITDLAPRN RALLAERDEI QGKLDAWHAE HPGANYDKAA YKSFLTEIGY LRPEPADFQI TTQNVDSEIA ETAGPQLVVP VMNARFAINA ANARWGSLYD ALYGTDAIPE DNGAEKGTGY NKVRGDKVIE WARNFLDDAV TLITGSHIGS TSYAIVDGEL EVGLEDGTTI GLADASQLVG YQGDPAKPTS ILLKHNGLHI DIQIDPESPI GSTDTAGIKD IVLESAVTTI MDFEDSVAAV DAEDKVLCYH NWLGLMQGTL AEEVSKGGKT FTRTMNPDRV YTALDGSELR LHGRSLLFVR NVGHLMTSDA ILDAQGNEVP EGIMDGLITS LIAKHSLRED VELKNSRTGS VYIVKPKMHG PDEVAFTNEL FGRIEDVLGL ARNTLKVGIM DEERRTTVNL KACIEAAKER VVFINTGFLD RTGDEIHTSM EAGPMVRKAD MKSQQWIASY EDWNVDTGLA TGLPGKAQIG KGMWAMPDLM ADMLAQKIGH PKSGANTAWV PSPTAATLHA THYHLVDVFK RQAEIAKGGR RASVDEILEI PLAANPNWSP EEIRQELDNN SQSILGYVVR WIDQGVGCSK VPDIKDVALM EDRATLRISS QLMANWLRHG IVTADEVVAS LERMAPVVDR QNAGDPNYRP MAPDFDGSIA FQAAKELILE GTKQPNGYTE PILHRRRREA KALSRV //