MASZ_MYCLB
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 03-AUG-2022, entry version 76.
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=MLBr02069;
OS Mycobacterium leprae (strain Br4923).
OC Bacteria; Actinobacteria; Corynebacteriales; 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}.
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DR EMBL; FM211192; CAR72166.1; -; Genomic_DNA.
DR RefSeq; WP_012634443.1; NC_011896.1.
DR PDB; 4EX4; X-ray; 2.10 A; A/B=1-731.
DR PDBsum; 4EX4; -.
DR AlphaFoldDB; B8ZSN3; -.
DR SMR; B8ZSN3; -.
DR EnsemblBacteria; CAR72166; CAR72166; MLBr02069.
DR KEGG; mlb:MLBr02069; -.
DR HOGENOM; CLU_028446_1_0_11; -.
DR OMA; MAPGFDG; -.
DR OrthoDB; 322024at2; -.
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; 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 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
