MASZ_PSEAE
ID MASZ_PSEAE Reviewed; 725 AA.
AC Q9I636;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=PA0482;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG03871.1; -; Genomic_DNA.
DR PIR; H83586; H83586.
DR RefSeq; NP_249173.1; NC_002516.2.
DR RefSeq; WP_003113258.1; NZ_QZGE01000010.1.
DR PDB; 5OAS; X-ray; 1.62 A; A=1-725.
DR PDB; 5VFB; X-ray; 1.36 A; A/B=1-725.
DR PDBsum; 5OAS; -.
DR PDBsum; 5VFB; -.
DR AlphaFoldDB; Q9I636; -.
DR SMR; Q9I636; -.
DR STRING; 287.DR97_3450; -.
DR PaxDb; Q9I636; -.
DR PRIDE; Q9I636; -.
DR EnsemblBacteria; AAG03871; AAG03871; PA0482.
DR GeneID; 879477; -.
DR KEGG; pae:PA0482; -.
DR PATRIC; fig|208964.12.peg.509; -.
DR PseudoCAP; PA0482; -.
DR HOGENOM; CLU_028446_1_0_6; -.
DR InParanoid; Q9I636; -.
DR OMA; MAPGFDG; -.
DR PhylomeDB; Q9I636; -.
DR BioCyc; PAER208964:G1FZ6-487-MON; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0004474; F:malate synthase activity; IBA:GO_Central.
DR GO; GO:0009436; P:glyoxylate catabolic process; IBA:GO_Central.
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..725
FT /note="Malate synthase G"
FT /id="PRO_0000166891"
FT ACT_SITE 340
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT ACT_SITE 631
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 617
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 14..22
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 32..69
FT /evidence="ECO:0007829|PDB:5VFB"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 138..143
FT /evidence="ECO:0007829|PDB:5VFB"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 162..179
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 229..235
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 238..244
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 267..274
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 282..296
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 361..377
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 391..395
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 401..418
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 425..431
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 434..437
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 440..445
FT /evidence="ECO:0007829|PDB:5VFB"
FT TURN 446..450
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 451..456
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 458..468
FT /evidence="ECO:0007829|PDB:5VFB"
FT TURN 469..472
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 478..483
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 485..500
FT /evidence="ECO:0007829|PDB:5VFB"
FT TURN 504..506
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 507..513
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 520..526
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 529..532
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 536..542
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 543..555
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 558..564
FT /evidence="ECO:0007829|PDB:5VFB"
FT TURN 565..567
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 573..576
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 589..613
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 618..621
FT /evidence="ECO:0007829|PDB:5VFB"
FT STRAND 627..630
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 632..647
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 653..671
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 684..686
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 688..698
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 700..702
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 704..706
FT /evidence="ECO:0007829|PDB:5VFB"
FT HELIX 709..722
FT /evidence="ECO:0007829|PDB:5VFB"
SQ SEQUENCE 725 AA; 78660 MW; 3669670A9E38D391 CRC64;
MTERVQVGGL QVAKVLFDFV NNEAIPGTGV SADTFWTGAE AVINDLAPKN KALLAKRDEL
QAKIDGWHQA RAGQAHDAVA YKAFLEEIGY LLPEAEDFQA GTQNVDDEIA RMAGPQLVVP
VMNARFALNA SNARWGSLYD ALYGTDVISE EGGAEKGKGY NKVRGDKVIA FARAFLDEAA
PLESGSHVDA TSYSVKNGAL VVALKNGSET GLKNAGQFLA FQGDAAKPQA VLLKHNGLHF
EIQIDPSSPV GQTDAAGVKD VLMEAALTTI MDCEDSVAAV DADDKVVIYR NWLGLMKGDL
AEEVSKGGST FTRTMNPDRV YTRADGSELT LHGRSLLFVR NVGHLMTNDA ILDKDGNEVP
EGIQDGLFTS LIAIHDLNGN TSRKNSRTGS VYIVKPKMHG PEEAAFTNEL FGRVEDVLGL
PRNTLKVGIM DEERRTTVNL KACIKAAKDR VVFINTGFLD RTGDEIHTSM EAGAVVRKGA
MKSEKWIGAY ENNNVDVGLA TGLQGKAQIG KGMWAMPDLM AAMLEQKIGH PLAGANTAWV
PSPTAATLHA LHYHKVDVFA RQAELAKRTP ASVDDILTIP LAPNTNWTAE EIKNEVDNNA
QGILGYVVRW IDQGVGCSKV PDINDVGLME DRATLRISSQ LLANWLRHGV ISQEQVVESL
KRMAVVVDRQ NASDPSYRPM APNFDDNVAF QAALELVVEG TRQPNGYTEP VLHRRRREFK
AKNGL
