(data stored in SCRATCH zone)

SWISSPROT: E6V4E7_VARPE

ID   E6V4E7_VARPE            Unreviewed;       724 AA.
AC   E6V4E7;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=Malate synthase G {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572};
DE            EC=2.3.3.9 {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572};
GN   Name=glcB {ECO:0000256|HAMAP-Rule:MF_00641};
GN   OrderedLocusNames=Varpa_0471 {ECO:0000313|EMBL:ADU34693.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34693.1, ECO:0000313|Proteomes:UP000008917};
RN   [1] {ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P.,
RA   Han J.-I.G., Woyke T.;
RT   "Complete sequence of Variovorax paradoxus EPS.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU34693.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34693.1,
RC   ECO:0000313|Proteomes:UP000008917};
RX   PubMed=24158554;
RA   Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA   Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT   "Genome of the Root-Associated Plant Growth-Promoting Bacterium
RT   Variovorax paradoxus Strain EPS.";
RL   Genome Announc. 1:e00843-13(2013).
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:0000256|HAMAP-Rule:MF_00641, ECO:0000256|SAAS:SAAS00058688}.
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:0000256|HAMAP-
CC         Rule:MF_00641, ECO:0000256|RuleBase:RU003572,
CC         ECO:0000256|SAAS:SAAS01118129};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00641, ECO:0000256|SAAS:SAAS00170223};
CC   -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate
CC       from isocitrate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00641,
CC       ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS00013009}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00641}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00641,
CC       ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS00013007}.
CC   -!- SIMILARITY: Belongs to the malate synthase family. GlcB subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572,
CC       ECO:0000256|SAAS:SAAS00539887}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00641}.
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DR   EMBL; CP002417; ADU34693.1; -; Genomic_DNA.
DR   RefSeq; WP_013538939.1; NC_014931.1.
DR   STRING; 595537.Varpa_0471; -.
DR   EnsemblBacteria; ADU34693; ADU34693; Varpa_0471.
DR   GeneID; 29719026; -.
DR   KEGG; vpe:Varpa_0471; -.
DR   eggNOG; ENOG4107QP3; Bacteria.
DR   eggNOG; COG2225; LUCA.
DR   HOGENOM; HOG000220740; -.
DR   KO; K01638; -.
DR   OMA; TEPVLHA; -.
DR   OrthoDB; 322024at2; -.
DR   BioCyc; VPAR595537:G1GQO-472-MONOMER; -.
DR   UniPathway; UPA00703; UER00720.
DR   Proteomes; UP000008917; 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   Gene3D; 2.170.170.11; -; 1.
DR   HAMAP; MF_00641; Malate_synth_G; 1.
DR   InterPro; IPR011076; Malate_synth-like_sf.
DR   InterPro; IPR023310; Malate_synth_G_beta_sub_dom.
DR   InterPro; IPR001465; Malate_synthase.
DR   InterPro; IPR006253; Malate_synthG.
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;
DR   PRODOM; E6V4E7.
DR   SWISS-2DPAGE; E6V4E7.
KW   Acyltransferase {ECO:0000313|EMBL:ADU34693.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008917};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00641,
KW   ECO:0000256|SAAS:SAAS00013017};
KW   Glyoxylate bypass {ECO:0000256|HAMAP-Rule:MF_00641,
KW   ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS00422331};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00641,
KW   ECO:0000256|SAAS:SAAS00058689};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00641,
KW   ECO:0000256|SAAS:SAAS00058684};
KW   Oxidation {ECO:0000256|HAMAP-Rule:MF_00641};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008917};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00641,
KW   ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS00078458,
KW   ECO:0000313|EMBL:ADU34693.1};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00641,
KW   ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS00422324}.
FT   REGION      125    126       Acetyl-CoA binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00641}.
FT   REGION      453    456       Glyoxylate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00641}.
FT   ACT_SITE    339    339       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641, ECO:0000256|PIRSR:PIRSR601465-
FT                                50}.
FT   ACT_SITE    632    632       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641, ECO:0000256|PIRSR:PIRSR601465-
FT                                50}.
FT   METAL       428    428       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641}.
FT   METAL       456    456       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641}.
FT   BINDING     118    118       Acetyl-CoA; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00641}.
FT   BINDING     275    275       Acetyl-CoA. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641}.
FT   BINDING     312    312       Acetyl-CoA. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641}.
FT   BINDING     339    339       Glyoxylate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641}.
FT   BINDING     428    428       Glyoxylate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641}.
FT   BINDING     537    537       Acetyl-CoA; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00641}.
FT   MOD_RES     618    618       Cysteine sulfenic acid (-SOH).
FT                                {ECO:0000256|HAMAP-Rule:MF_00641}.
SQ   SEQUENCE   724 AA;  77686 MW;  6C1FA1D4359D8617 CRC64;
     MTARTTAHGL QVATELHRFI EEKVLPATGV ASDVFWKGFD AIVSDLAPKN IALLAERDRL
     QSELDAWHKK NPGPIADMPA YRAFLEKIGY LLPQPKGAKA TTANVDSELA LQAGPQLVVP
     ILNARYALNA ANARWGSLYD ALYGTDAIPE TGGAEKGKGY NPVRGAKVIE FARNVLDQAA
     PLANGSHKMA TGYSVKDGKL VVALQSSSTG LADPAQFIGY QGDAAAPSSV LLKHNGIHLD
     IRIDRSTAIG KTDAAGVSDL VLEAALSTIL DLEDSVAVVD AADKVVAYAN WLGIVEGTLT
     EEVAKGGKTF TRGLNADREY TGADGQPVKL HGRSLMFLRN VGHLMTNPAI LYAGGKEIPE
     GILDAVVTTT IATIDLKRKG NSRTGSIYIV KPKMHGPAEV AFASELFGRV EQLLGLPANT
     VKLGIMDEER RTSVNLKACI AEAAARVAFI NTGFLDRTGD EMHTAMQGGP MIRKGDMKSS
     AWIGAYEKNN VLVGLSCGLR GKAQIGKGMW AMPDLMAAML EQKIGHPKAG ANTAWVPSPT
     AATLHALHYH QVSVTAVQQE LEKIDADAER DNILNALLQV PIAPEAKWTA EERQQEIDNN
     VQGILGYVVR WIDQGVGCSK VPDIHNVGLM EDRATLRISS QHIANWLLHG VVTKAQVDET
     FQRMAKVVDE QNAGDALYQP MAGNFATSAA YKAAQDLVFK GIEQPSGYTE PLLHAWRLKV
     KGEA
//

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