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Database: UniProt/SWISS-PROT
Entry: MASZ_OCHA4
LinkDB: MASZ_OCHA4
Original site: MASZ_OCHA4 
ID   MASZ_OCHA4              Reviewed;         728 AA.
AC   A6WYD2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   29-OCT-2014, entry version 49.
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=Oant_1269;
OS   Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / NCTC 12168).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Ochrobactrum.
OX   NCBI_TaxID=439375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49188 / DSM 6882 / NCTC 12168;
RX   PubMed=21685287; DOI=10.1128/JB.05335-11;
RA   Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M.,
RA   Shin M., Ugalde R.A., Garcia E., Tolmasky M.E.;
RT   "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile
RT   opportunistic pathogen and symbiont of several eukaryotic hosts.";
RL   J. Bacteriol. 193:4274-4275(2011).
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: Magnesium. {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}.
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DR   EMBL; CP000758; ABS13986.1; -; Genomic_DNA.
DR   RefSeq; WP_012091375.1; NC_009667.1.
DR   RefSeq; YP_001369815.1; NC_009667.1.
DR   ProteinModelPortal; A6WYD2; -.
DR   SMR; A6WYD2; 10-728.
DR   STRING; 439375.Oant_1269; -.
DR   EnsemblBacteria; ABS13986; ABS13986; Oant_1269.
DR   GeneID; 5378625; -.
DR   KEGG; oan:Oant_1269; -.
DR   PATRIC; 20467633; VBIOchAnt73124_1330.
DR   eggNOG; COG2225; -.
DR   HOGENOM; HOG000220740; -.
DR   KO; K01638; -.
DR   OMA; SQFIENE; -.
DR   OrthoDB; EOG6HJ286; -.
DR   BioCyc; OANT439375:GJIT-1286-MONOMER; -.
DR   UniPathway; UPA00703; UER00720.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004474; F:malate synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   Gene3D; 2.170.170.11; -; 2.
DR   HAMAP; MF_00641; Malate_synth_G; 1.
DR   InterPro; IPR011076; Malate_synth-like.
DR   InterPro; IPR023310; Malate_synth_G_beta_sub_dom.
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;
KW   Complete proteome; Cytoplasm; Glyoxylate bypass; Magnesium;
KW   Metal-binding; Oxidation; Reference proteome; Transferase;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    728       Malate synthase G.
FT                                /FTId=PRO_1000056916.
FT   REGION      130    131       Acetyl-CoA binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00641}.
FT   REGION      462    465       Glyoxylate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00641}.
FT   ACT_SITE    345    345       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00641}.
FT   ACT_SITE    636    636       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00641}.
FT   METAL       437    437       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00641}.
FT   METAL       465    465       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00641}.
FT   BINDING     123    123       Acetyl-CoA; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00641}.
FT   BINDING     281    281       Acetyl-CoA. {ECO:0000255|HAMAP-
FT                                Rule:MF_00641}.
FT   BINDING     318    318       Acetyl-CoA. {ECO:0000255|HAMAP-
FT                                Rule:MF_00641}.
FT   BINDING     345    345       Glyoxylate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00641}.
FT   BINDING     437    437       Glyoxylate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00641}.
FT   BINDING     546    546       Acetyl-CoA; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00641}.
FT   MOD_RES     622    622       Cysteine sulfenic acid (-SOH).
FT                                {ECO:0000255|HAMAP-Rule:MF_00641}.
SQ   SEQUENCE   728 AA;  79664 MW;  89C758B66592CB10 CRC64;
     MVSQKAGNYV EIEGLRVAPE LVEFLAKEAA PGTGVEPEKF WKGFAAIIRD LAPKNRALLA
     KRDDLQAKID AWYKQNRDKG YSQADYQQFL KNIGYLLPEG GEFSVSTTNV DPEITHIAGP
     QLVVPVMNAR YALNAANARW GSLYDALYGT DAISDADGGE KGKGYNPKRG EKVIAWAKNF
     LDESAPLATG NWANVAGLAV KDGKLEIKLT DGSATALKDA NQFKGYNGDA AAPTNVLLAK
     NNMHVDIVVN ADHPIGKTDP AHIADVVLES AVSTIQDCED SIAAVDAEDK VAVYRNWLGL
     MNGKLEDTFE KNGKQMTRRL NGDRSYKAAD GSTLSLKGRS LMLVRNVGHL MTNPAIIDAD
     GHEVPEGIMD AAFTSLIALH DIGPNGRHMN SREGSVYIVK PKMHGPEEVA FANEIFTRTE
     EMLGMKPNTL KIGIMDEERR TTVNLKEAIR AAKERVVFIN TGFLDRTGDE IHTSMEAGPM
     IRKGDMKQAA WIGAYEQWNV DIGLECGLSG HAQIGKGMWA MPDLMAAMLE QKIAHPKAGA
     NTAWVPSPTA ATLHATHYHQ VDVAAVQAKL KSRPRAKLDD ILSVPVATRP NWTPEDIQHE
     IDNNAQGILG YVVRWVDQGV GCSKVPDINN VGLMEDRATL RISAQHIANW LYHGVVSEAQ
     VMETMKRMAA VVDKQNEGDA LYRPMAADFD KSIAFQAACD LVFKGREQPN GYTEPVLHRR
     RLELKAQG
//
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