(data stored in SCRATCH zone)

SWISSPROT: E6V4B6_VARPE

ID   E6V4B6_VARPE            Unreviewed;       435 AA.
AC   E6V4B6;
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=Glucose-1-phosphate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00624};
DE            EC=2.7.7.27 {ECO:0000256|HAMAP-Rule:MF_00624};
DE   AltName: Full=ADP-glucose pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00624};
DE            Short=ADPGlc PPase {ECO:0000256|HAMAP-Rule:MF_00624};
DE   AltName: Full=ADP-glucose synthase {ECO:0000256|HAMAP-Rule:MF_00624};
GN   Name=glgC {ECO:0000256|HAMAP-Rule:MF_00624};
GN   OrderedLocusNames=Varpa_0440 {ECO:0000313|EMBL:ADU34662.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34662.1, 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:ADU34662.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34662.1,
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 biosynthesis of ADP-glucose, a building
CC       block required for the elongation reactions to produce glycogen.
CC       Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate
CC       (G1P) to produce pyrophosphate and ADP-Glc. {ECO:0000256|HAMAP-
CC       Rule:MF_00624}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-
CC         glucose + diphosphate; Xref=Rhea:RHEA:12120, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57498,
CC         ChEBI:CHEBI:58601; EC=2.7.7.27; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00624, ECO:0000256|SAAS:SAAS01122021};
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00624, ECO:0000256|RuleBase:RU003742,
CC       ECO:0000256|SAAS:SAAS00015082}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00624}.
CC   -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC       adenylyltransferase family. {ECO:0000256|HAMAP-Rule:MF_00624,
CC       ECO:0000256|SAAS:SAAS00569693}.
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DR   EMBL; CP002417; ADU34662.1; -; Genomic_DNA.
DR   RefSeq; WP_013538908.1; NC_014931.1.
DR   STRING; 595537.Varpa_0440; -.
DR   EnsemblBacteria; ADU34662; ADU34662; Varpa_0440.
DR   GeneID; 29714524; -.
DR   KEGG; vpe:Varpa_0440; -.
DR   eggNOG; ENOG4107QQ4; Bacteria.
DR   eggNOG; COG0448; LUCA.
DR   HOGENOM; HOG000278607; -.
DR   KO; K00975; -.
DR   OMA; HCVLGVR; -.
DR   OrthoDB; 1557977at2; -.
DR   BioCyc; VPAR595537:G1GQO-442-MONOMER; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000008917; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.550.10; -; 1.
DR   HAMAP; MF_00624; GlgC; 1.
DR   InterPro; IPR011831; ADP-Glc_PPase.
DR   InterPro; IPR005836; ADP_Glu_pyroP_CS.
DR   InterPro; IPR023049; GlgC_bac.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR02091; glgC; 1.
DR   PROSITE; PS00808; ADP_GLC_PYROPHOSPH_1; 1.
DR   PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1.
DR   PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; E6V4B6.
DR   SWISS-2DPAGE; E6V4B6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00624,
KW   ECO:0000256|SAAS:SAAS00458608};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00624,
KW   ECO:0000256|SAAS:SAAS00423450};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008917};
KW   Glycogen biosynthesis {ECO:0000256|HAMAP-Rule:MF_00624,
KW   ECO:0000256|RuleBase:RU003742, ECO:0000256|SAAS:SAAS00087462};
KW   Glycogen metabolism {ECO:0000256|HAMAP-Rule:MF_00624,
KW   ECO:0000256|SAAS:SAAS00015095};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00624,
KW   ECO:0000256|SAAS:SAAS00458574};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00624,
KW   ECO:0000256|SAAS:SAAS00189090, ECO:0000313|EMBL:ADU34662.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008917};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00624,
KW   ECO:0000256|SAAS:SAAS00189093, ECO:0000313|EMBL:ADU34662.1}.
FT   DOMAIN       25    299       NTP_transferase. {ECO:0000259|Pfam:
FT                                PF00483}.
FT   REGION      199    200       Alpha-D-glucose 1-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00624}.
FT   BINDING     117    117       Alpha-D-glucose 1-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00624}.
FT   BINDING     184    184       Alpha-D-glucose 1-phosphate; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00624}.
FT   BINDING     217    217       Alpha-D-glucose 1-phosphate; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00624}.
FT   SITE         77     77       Could play a key role in the
FT                                communication between the regulatory and
FT                                the substrate sites. {ECO:0000256|HAMAP-
FT                                Rule:MF_00624}.
FT   SITE        116    116       Could play a key role in the
FT                                communication between the regulatory and
FT                                the substrate sites. {ECO:0000256|HAMAP-
FT                                Rule:MF_00624}.
SQ   SEQUENCE   435 AA;  48018 MW;  149EB77DE86A6F86 CRC64;
     MDNKLGTPPS QEPLQAHQLV RRTIALVLAG GRGSRLKQLT DRRAKPAVYF GGKFRIIDFA
     LSNCLNSGIR RMAVVTQYKS HSLMRHLQRG WSFLRAELNE MVDVLPAQQR VGDEHWYRGT
     ADAVFQNLDI IQTRSTKHDY VVVLAGDHIY KMDYSIMVKD HAERGLGCTV GCIEVPRMEA
     TAFGVMAIDD GRQITAFLEK PADPPAMPGH PDVALASMGI YVFDSNYLYQ LLEEDAANPD
     SSHDFGKDII PRAVAQGRAL AHPFGMSCVT RASRGPDAKA YWRDVGTIDA FWAANLDLAS
     ITPELDIYDT DWPIWTYQRQ LPPAKFVLDR DGKHGMTVNT IVSGGCIVSG SKVSSSVLFS
     GVRIHSFCEI NEAVLLPDVE VGRGARLSKV VIDRGCVIPD DMVIGEDAAA DAARFERTET
     GVVLVTREML KRLTA
//

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