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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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