MASZ_SHIFL
ID MASZ_SHIFL Reviewed; 723 AA.
AC P59663;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
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=SF3015, S3216;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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}.
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; AE005674; AAN44496.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18307.1; -; Genomic_DNA.
DR RefSeq; NP_708789.1; NC_004337.2.
DR RefSeq; WP_000084122.1; NZ_WPGW01000053.1.
DR AlphaFoldDB; P59663; -.
DR BMRB; P59663; -.
DR SMR; P59663; -.
DR STRING; 198214.SF3015; -.
DR EnsemblBacteria; AAN44496; AAN44496; SF3015.
DR EnsemblBacteria; AAP18307; AAP18307; S3216.
DR GeneID; 1026622; -.
DR KEGG; sfl:SF3015; -.
DR KEGG; sfx:S3216; -.
DR PATRIC; fig|198214.7.peg.3586; -.
DR HOGENOM; CLU_028446_1_0_6; -.
DR OMA; FWRNVDE; -.
DR OrthoDB; 322024at2; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 3: Inferred from homology;
KW Cytoplasm; Glyoxylate bypass; Magnesium; Metal-binding; Oxidation;
KW Reference proteome; Transferase; Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..723
FT /note="Malate synthase G"
FT /id="PRO_0000166900"
FT ACT_SITE 338
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 274
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 311
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 338
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 427
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 427
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 452..455
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT BINDING 536
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 MOD_RES 688
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
SQ SEQUENCE 723 AA; 80362 MW; 048288575D389BF0 CRC64;
MSQTITQGRL RIDANFKRFV DGEVLPGVEL DAAAFWHNVD EIVHDLAPEN RQLLAERDRI
QAALDEWHRS NPGPVKDKAA YKSFLRELGY LVPQPERVTV ETTGIDSEIT SQAGPQLVVP
AMNARYALNA ANARWGSLYD ALYGSDIIPQ EGAMVSGYDP QRGEQVIAWV RRFLDESLPL
ENGSYQDVVA FKVVDKQLRI QLKNGKETTL RTPAQFVGYR GDAAAPTCIL LKNNGLHIEL
QIDANGRIGK DDPAHINDVI VEAAISTILD CEDSVAAVDA EDKILLYRNL LGLMQGTLQE
KMEKNGRQIV RKLNDDRQYT AADGSEISLH GRSLLFIRNV GHLMTIPVIW DSEGNEIPEG
ILDGVMTGAI ALYDLKVQKN SRTGSVYIVK PKMHGPQEVA FANKLFTRIE TMLGMAPNTL
KMGIMDEERR TSLNLRSCIA QARNRVAFIN TGFLDRTGDE MHSVMEAGPM LRKNQMKSTP
WIKAYERNNV LSGLFCGLRG KAQIGKGMWA MPDLMADMYS QKGDQLRAGA NTAWVPSPTA
ATLHALHYHH TNVQSVQANI AQTEFSAEFE PLLDDLLTIP VAENANWSAQ EIQQELDNNV
QGILGYVVRW VEQGIGCSKV PDIHNVALME DRATLRISSQ HIANWLRHGI LTKEQVQASL
ENMAKVVDQQ NAGDPAYRPM AGNFANSCAF KAASDLIFLG VKQPNGYTEP LLHAWRLREK
ESH
