MASZ_MYCTO
ID MASZ_MYCTO Reviewed; 741 AA.
AC P9WK16; L0T815; P0A5J4; Q50596;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
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=MT1885;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH SUBSTRATES AND
RP MAGNESIUM ION, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, REACTION
RP MECHANISM, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR,
RP AND SUBUNIT.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12393860; DOI=10.1074/jbc.m209248200;
RA Smith C.V., Huang C.C., Miczak A., Russell D.G., Sacchettini J.C.,
RA Honer zu Bentrup K.;
RT "Biochemical and structural studies of malate synthase from Mycobacterium
RT tuberculosis.";
RL J. Biol. Chem. 278:1735-1743(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, ECO:0000269|PubMed:12393860}.
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, ECO:0000269|PubMed:12393860};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00641,
CC ECO:0000269|PubMed:12393860};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00641,
CC ECO:0000269|PubMed:12393860};
CC Note=Mg(2+). Mn(2+) is able to replace Mg(2+). {ECO:0000255|HAMAP-
CC Rule:MF_00641, ECO:0000269|PubMed:12393860};
CC -!- ACTIVITY REGULATION: By bromopyruvate, oxalate, and
CC phosphoenolpyruvate. Malate inhibits the activity to 50% at 1 mM
CC concentration. Glycolate inhibits only at fairly high concentrations.
CC {ECO:0000269|PubMed:12393860}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30 uM for acetyl-CoA (at pH 7.5) {ECO:0000269|PubMed:12393860};
CC KM=57 uM for glyoxylate (at pH 7.5) {ECO:0000269|PubMed:12393860};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:12393860};
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|PubMed:12393860}.
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; AE000516; AAK46156.1; -; Genomic_DNA.
DR PIR; F70722; F70722.
DR RefSeq; WP_003409271.1; NZ_KK341227.1.
DR PDB; 1N8I; X-ray; 2.10 A; A=1-741.
DR PDB; 1N8W; X-ray; 2.70 A; A/B=1-741.
DR PDBsum; 1N8I; -.
DR PDBsum; 1N8W; -.
DR AlphaFoldDB; P9WK16; -.
DR SMR; P9WK16; -.
DR EnsemblBacteria; AAK46156; AAK46156; MT1885.
DR KEGG; mtc:MT1885; -.
DR PATRIC; fig|83331.31.peg.2029; -.
DR HOGENOM; CLU_028446_1_0_11; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0009986; C:cell surface; IDA:CAFA.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IDA:CAFA.
DR GO; GO:0004474; F:malate synthase activity; IDA:CAFA.
DR GO; GO:0030145; F:manganese ion binding; IDA:CAFA.
DR GO; GO:0006097; P:glyoxylate cycle; IDA:CAFA.
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..741
FT /note="Malate synthase G"
FT /id="PRO_0000427732"
FT REGION 718..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 339
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641,
FT ECO:0000269|PubMed:12393860"
FT ACT_SITE 633
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641,
FT ECO:0000269|PubMed:12393860"
FT BINDING 118
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT BINDING 125..129
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT BINDING 275
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT BINDING 305
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT BINDING 312
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT BINDING 339
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT BINDING 434
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT BINDING 434
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 459..462
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 543
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT BINDING 618..621
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT BINDING 633
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT MOD_RES 619
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 14..22
FT /evidence="ECO:0007829|PDB:1N8I"
FT TURN 26..29
FT /evidence="ECO:0007829|PDB:1N8W"
FT HELIX 32..69
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 138..143
FT /evidence="ECO:0007829|PDB:1N8I"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:1N8W"
FT HELIX 162..179
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 226..234
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 281..295
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:1N8W"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 346..352
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:1N8W"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 360..372
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:1N8I"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:1N8W"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 393..397
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 403..420
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 427..433
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 436..439
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 442..448
FT /evidence="ECO:0007829|PDB:1N8I"
FT TURN 449..452
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 453..458
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 460..470
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 480..485
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 487..502
FT /evidence="ECO:0007829|PDB:1N8I"
FT TURN 506..508
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 509..513
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 522..528
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 531..534
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 538..544
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 545..557
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 560..567
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 575..578
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 591..615
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 620..623
FT /evidence="ECO:0007829|PDB:1N8I"
FT STRAND 629..632
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 634..649
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 655..672
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 686..688
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 690..700
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 702..704
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 706..708
FT /evidence="ECO:0007829|PDB:1N8I"
FT HELIX 711..726
FT /evidence="ECO:0007829|PDB:1N8I"
SQ SEQUENCE 741 AA; 80403 MW; A92F54E0FE8B7C64 CRC64;
MTDRVSVGNL RIARVLYDFV NNEALPGTDI DPDSFWAGVD KVVADLTPQN QALLNARDEL
QAQIDKWHRR RVIEPIDMDA YRQFLTEIGY LLPEPDDFTI TTSGVDAEIT TTAGPQLVVP
VLNARFALNA ANARWGSLYD ALYGTDVIPE TDGAEKGPTY NKVRGDKVIA YARKFLDDSV
PLSSGSFGDA TGFTVQDGQL VVALPDKSTG LANPGQFAGY TGAAESPTSV LLINHGLHIE
ILIDPESQVG TTDRAGVKDV ILESAITTIM DFEDSVAAVD AADKVLGYRN WLGLNKGDLA
AAVDKDGTAF LRVLNRDRNY TAPGGGQFTL PGRSLMFVRN VGHLMTNDAI VDTDGSEVFE
GIMDALFTGL IAIHGLKASD VNGPLINSRT GSIYIVKPKM HGPAEVAFTC ELFSRVEDVL
GLPQNTMKIG IMDEERRTTV NLKACIKAAA DRVVFINTGF LDRTGDEIHT SMEAGPMVRK
GTMKSQPWIL AYEDHNVDAG LAAGFSGRAQ VGKGMWTMTE LMADMVETKI AQPRAGASTA
WVPSPTAATL HALHYHQVDV AAVQQGLAGK RRATIEQLLT IPLAKELAWA PDEIREEVDN
NCQSILGYVV RWVDQGVGCS KVPDIHDVAL MEDRATLRIS SQLLANWLRH GVITSADVRA
SLERMAPLVD RQNAGDVAYR PMAPNFDDSI AFLAAQELIL SGAQQPNGYT EPILHRRRRE
FKARAAEKPA PSDRAGDDAA R
