ID MASZ_MYCLB Reviewed; 731 AA. AC B8ZSN3; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 83. 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=MLBr02069; OS Mycobacterium leprae (strain Br4923). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=561304; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Br4923; RX PubMed=19881526; DOI=10.1038/ng.477; RA Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A., RA Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C., RA Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H., RA Vera-Cabrera L., Stefani M.M., Banu S., Macdonald M., Sapkota B.R., RA Spencer J.S., Thomas J., Harshman K., Singh P., Busso P., Gattiker A., RA Rougemont J., Brennan P.J., Cole S.T.; RT "Comparative genomic and phylogeographic analysis of Mycobacterium RT leprae."; RL Nat. Genet. 41:1282-1289(2009). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH MAGNESIUM ION, AND RP SUBUNIT. RG Seattle structural genomics center for infectious disease (SSGCID); RT "The structure of glcb from mycobacterium leprae."; RL Submitted (APR-2012) to the PDB data bank. 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 -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from CC isocitrate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_00641}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.2}. 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; FM211192; CAR72166.1; -; Genomic_DNA. DR PDB; 4EX4; X-ray; 2.10 A; A/B=1-731. DR PDBsum; 4EX4; -. DR AlphaFoldDB; B8ZSN3; -. DR SMR; B8ZSN3; -. DR KEGG; mlb:MLBr02069; -. DR HOGENOM; CLU_028446_1_0_11; -. DR UniPathway; UPA00703; UER00720. DR Proteomes; UP000006900; 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 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Glyoxylate bypass; Magnesium; Metal-binding; KW Oxidation; Transferase; Tricarboxylic acid cycle. FT CHAIN 1..731 FT /note="Malate synthase G" FT /id="PRO_1000147426" FT ACT_SITE 340 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT ACT_SITE 638 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 439 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 439 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 464..467 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 467 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 548 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT MOD_RES 624 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT STRAND 4..7 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 10..13 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 14..23 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 32..70 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 78..87 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 107..110 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 116..120 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 124..132 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 135..137 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 138..143 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 162..179 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 187..189 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 207..209 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 214..216 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 217..220 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 232..235 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 238..243 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 251..253 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 260..264 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 267..274 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 282..297 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 302..306 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 309..313 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 319..322 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 328..331 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 336..340 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 347..353 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 359..364 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 365..377 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 378..380 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 385..387 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 394..396 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 398..402 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 408..425 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 432..438 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 441..444 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 447..453 FT /evidence="ECO:0007829|PDB:4EX4" FT TURN 454..457 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 458..463 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 465..475 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 477..479 FT /evidence="ECO:0007829|PDB:4EX4" FT TURN 485..487 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 488..490 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 492..507 FT /evidence="ECO:0007829|PDB:4EX4" FT TURN 511..513 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 514..518 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 523..525 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 527..533 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 536..539 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 543..549 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 550..562 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 565..572 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 580..583 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 596..620 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 625..628 FT /evidence="ECO:0007829|PDB:4EX4" FT STRAND 634..637 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 639..654 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 660..677 FT /evidence="ECO:0007829|PDB:4EX4" FT TURN 678..680 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 691..693 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 695..705 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 707..709 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 711..713 FT /evidence="ECO:0007829|PDB:4EX4" FT HELIX 716..728 FT /evidence="ECO:0007829|PDB:4EX4" SQ SEQUENCE 731 AA; 80143 MW; 3878C0DAE26DECDA CRC64; MTDRVSAGNL RVARVLYDFV NNEALPGTDI NPNSFWSGVA KVVADLTPQN QSLLNSRDEL QAQIDKWHRH RVIEPFDVDA YRQFLIDIGY LLPEPDDFTI STSGVDDEIT MTAGPQLVVP VLNARFALNA ANARWGSLYD ALYGTDTIPE TEGAEKGSEY NKIRGDKVIA YARKFMDQAV PLASDSWTNA TGVSIFDGQL QIAIGTNSTG LASPEKFVGY NRQLRSSNWS VLLANHGLHI EVLIDPESPI GKTDPVGIKD VILESAITTI MDFEDSVTAV DADDKVRGYR NWLGLNKGDL TEEVNKDGKT FTRVLNADRS YTTPDGGELT LPGRSLLFVR NVGHLTTSDA ILVDGGDGQE KEVFEGIIDA VFTGLAAIHG LKTGEANGPL TNSRTGSIYI VKPKMHGPAE VAFTCELFSR VEDVLGLPQG TLKVGIMDEE RRTTLNLKAC IKAAADRVVF INTGFLDRTG DEIHTSMEAG PMIRKGAMKN STWIKAYEDA NVDIGLAAGF KGKAQIGKGM WAMTELMADM VEQKIGQPKA GATTAWVPSP TAATLHAMHY HQVDVAAVQQ ELTGQRRATV DQLLTIPLAK ELAWAPEEIR EEVDNDCQSI LGYVVRWVDQ GIGCSKVPDI HNVALMEDRA TLRISSQLLA NWLRHGVITS EDVRASLERM APLVDQQNAE DPAYRPMAPN FDDSIAFLAA QELILSGAQQ PNGYTEPILH RRRREFKAQN R //