(data stored in ACNUC7421 zone)

SWISSPROT: MASZ_PSEAB

ID   MASZ_PSEAB              Reviewed;         725 AA.
AC   Q02TT1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   07-JUN-2017, entry version 72.
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=PA14_06290;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: Involved in the glycolate utilization. Catalyzes the
CC       condensation and subsequent hydrolysis of acetyl-coenzyme A
CC       (acetyl-CoA) and glyoxylate to form malate and CoA.
CC       {ECO:0000255|HAMAP-Rule:MF_00641}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + glyoxylate = (S)-malate +
CC       CoA. {ECO:0000255|HAMAP-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
CC       from 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}.
DR   EMBL; CP000438; ABJ15447.1; -; Genomic_DNA.
DR   RefSeq; WP_003105217.1; NC_008463.1.
DR   ProteinModelPortal; Q02TT1; -.
DR   SMR; Q02TT1; -.
DR   EnsemblBacteria; ABJ15447; ABJ15447; PA14_06290.
DR   KEGG; pau:PA14_06290; -.
DR   HOGENOM; HOG000220740; -.
DR   KO; K01638; -.
DR   OMA; GDEMHTS; -.
DR   UniPathway; UPA00703; UER00720.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004474; F:malate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   CDD; cd00728; malate_synt_G; 1.
DR   HAMAP; MF_00641; Malate_synth_G; 1.
DR   InterPro; IPR011076; Malate_synth-like.
DR   InterPro; IPR001465; Malate_synthase.
DR   InterPro; IPR006253; Malate_synthG.
DR   Pfam; PF01274; Malate_synthase; 1.
DR   SUPFAM; SSF51645; SSF51645; 1.
DR   TIGRFAMs; TIGR01345; malate_syn_G; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q02TT1.
DR   SWISS-2DPAGE; Q02TT1.
KW   Complete proteome; Cytoplasm; Glyoxylate bypass; Magnesium;
KW   Metal-binding; Oxidation; Transferase; Tricarboxylic acid cycle.
FT   CHAIN         1    725       Malate synthase G.
FT                                /FTId=PRO_1000056918.
FT   REGION      125    126       Acetyl-CoA binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00641}.
FT   REGION      457    460       Glyoxylate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00641}.
FT   ACT_SITE    340    340       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00641}.
FT   ACT_SITE    631    631       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00641}.
FT   METAL       432    432       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00641}.
FT   METAL       460    460       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00641}.
FT   BINDING     118    118       Acetyl-CoA; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00641}.
FT   BINDING     276    276       Acetyl-CoA. {ECO:0000255|HAMAP-
FT                                Rule:MF_00641}.
FT   BINDING     313    313       Acetyl-CoA. {ECO:0000255|HAMAP-
FT                                Rule:MF_00641}.
FT   BINDING     340    340       Glyoxylate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00641}.
FT   BINDING     432    432       Glyoxylate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00641}.
FT   BINDING     541    541       Acetyl-CoA; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00641}.
FT   MOD_RES     617    617       Cysteine sulfenic acid (-SOH).
FT                                {ECO:0000255|HAMAP-Rule:MF_00641}.
SQ   SEQUENCE   725 AA;  78632 MW;  CEC503219946E5CE CRC64;
     MTERVQVGGL QVAKVLFDFV NNEAIPGTGV SADTFWTGAE AVINDLAPKN KALLAKRDEL
     QAKIDGWHQA RAGQAHDAAA 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
//

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