MASZ_MYCMM
ID MASZ_MYCMM Reviewed; 731 AA.
AC B2HSY2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=MMAR_2713;
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=216594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M;
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
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 Evidence={ECO:0000255|HAMAP-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}.
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DR EMBL; CP000854; ACC41156.1; -; Genomic_DNA.
DR RefSeq; WP_012394427.1; NC_010612.1.
DR PDB; 6AXE; X-ray; 1.60 A; A/B=1-731.
DR PDBsum; 6AXE; -.
DR AlphaFoldDB; B2HSY2; -.
DR SMR; B2HSY2; -.
DR STRING; 216594.MMAR_2713; -.
DR EnsemblBacteria; ACC41156; ACC41156; MMAR_2713.
DR KEGG; mmi:MMAR_2713; -.
DR eggNOG; COG2225; Bacteria.
DR HOGENOM; CLU_028446_1_0_11; -.
DR OMA; MAPGFDG; -.
DR OrthoDB; 322024at2; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000001190; 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; Reference proteome; Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..731
FT /note="Malate synthase G"
FT /id="PRO_1000130893"
FT ACT_SITE 339
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT ACT_SITE 637
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 275
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 312
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 339
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 438
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 438
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 463..466
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 547
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT MOD_RES 623
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 14..22
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 32..69
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 138..143
FT /evidence="ECO:0007829|PDB:6AXE"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 162..179
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 224..234
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 281..296
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 325..330
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 346..352
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 358..363
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 364..376
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:6AXE"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 397..401
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 407..424
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 431..437
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 440..443
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 446..452
FT /evidence="ECO:0007829|PDB:6AXE"
FT TURN 453..456
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 457..462
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 464..474
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 484..489
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 491..506
FT /evidence="ECO:0007829|PDB:6AXE"
FT TURN 510..512
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 513..517
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 526..532
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 535..538
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 542..548
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 549..561
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 564..571
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 579..582
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 595..619
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 624..627
FT /evidence="ECO:0007829|PDB:6AXE"
FT STRAND 633..636
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 638..653
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 659..676
FT /evidence="ECO:0007829|PDB:6AXE"
FT TURN 677..679
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 690..692
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 694..704
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 706..708
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 710..712
FT /evidence="ECO:0007829|PDB:6AXE"
FT HELIX 715..729
FT /evidence="ECO:0007829|PDB:6AXE"
SQ SEQUENCE 731 AA; 79479 MW; B1E03DE79642E7DC CRC64;
MTDRVSAGNL RVARVLYDFV NNEALPGTDI DQDSFWAGVD KVVTDLTPQN QDLLKTRDDL
QAQIDKWHRH RVIEPLDPQA YREFLTEIGY LLPAPEDFTI TTSGVDDEIT TTAGPQLVVP
ILNARFALNA ANARWGSLYD ALYGTDVISE SDGAEKGRGY NKVRGDKVIA YARQFLDDSV
PLAGASYTDA TGFKVEDGQL VVSLADTSAA LADPGQFAGY TGTAENPKSI LLANHGLHIE
ILIDPESQIG ATDGAGVKDV ILESAITTIM DFEDSVAAVD ADDKVLGYRN WLGLNRGDLS
EDVTKDDKTF TRVLNTDRTY TAPHGGELTL PGRSLLFVRN VGHLMTNDAI VSDAEGAEGA
PVFEGIMDAL FTGLIAIHGL RSTDANGLLT NSRTGSIYIV KPKMHGPAEV AFTCELFSRV
EDVLGLPQGT MKVGIMDEER RTTLNLKACI KAAADRVVFI NTGFLDRTGD EIHTSMEAGP
MIRKGAMKNT AWIKAYEDAN VDTGLAAGFS GKAQIGKGMW AMTELMADMV EQKIAQPKAG
ATTAWVPSPT AATLHAMHYH KVDVFAVQKE LQGKTRTSVD ELLTIPLAKE LAWAPEEIRE
EVDNNCQSIL GYVVRWIDQG VGCSKVPDIH NVALMEDRAT LRISSQLLAN WLRHGVITSE
DARASLERMA PLVDKQNAGD PEYHAMAPNF DDSIAFLAAQ DLILSGAQQP NGYTEPILHR
RRRELKARAG A
