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Database: UniProt
Entry: Q9KDX4
LinkDB: Q9KDX4
Original site: Q9KDX4 
ID   GLGC_BACHD              Reviewed;         383 AA.
AC   Q9KDX4;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-OCT-2017, entry version 96.
DE   RecName: Full=Glucose-1-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00624};
DE            EC=2.7.7.27 {ECO:0000255|HAMAP-Rule:MF_00624};
DE   AltName: Full=ADP-glucose pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00624};
DE            Short=ADPGlc PPase {ECO:0000255|HAMAP-Rule:MF_00624};
DE   AltName: Full=ADP-glucose synthase {ECO:0000255|HAMAP-Rule:MF_00624};
GN   Name=glgC {ECO:0000255|HAMAP-Rule:MF_00624}; OrderedLocusNames=BH1087;
OS   Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM
OS   9153 / C-125).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N.,
RA   Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S.,
RA   Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus
RT   halodurans and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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:0000255|HAMAP-
CC       Rule:MF_00624}.
CC   -!- CATALYTIC ACTIVITY: ATP + alpha-D-glucose 1-phosphate =
CC       diphosphate + ADP-glucose. {ECO:0000255|HAMAP-Rule:MF_00624}.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00624}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00624}.
CC   -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC       adenylyltransferase family. {ECO:0000255|HAMAP-Rule:MF_00624}.
DR   EMBL; BA000004; BAB04806.1; -; Genomic_DNA.
DR   PIR; G83785; G83785.
DR   ProteinModelPortal; Q9KDX4; -.
DR   SMR; Q9KDX4; -.
DR   STRING; 272558.BH1087; -.
DR   DNASU; 892001; -.
DR   EnsemblBacteria; BAB04806; BAB04806; BAB04806.
DR   KEGG; bha:BH1087; -.
DR   eggNOG; ENOG4105CNB; Bacteria.
DR   eggNOG; COG0448; LUCA.
DR   HOGENOM; HOG000278603; -.
DR   KO; K00975; -.
DR   OMA; HCVLGVR; -.
DR   OrthoDB; POG091H09L2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001258; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
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.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   SUPFAM; SSF53448; SSF53448; 2.
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;
KW   ATP-binding; Carbohydrate metabolism; Complete proteome;
KW   Glycogen biosynthesis; Glycogen metabolism; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN         1    383       Glucose-1-phosphate adenylyltransferase.
FT                                /FTId=PRO_0000195280.
FT   REGION      179    180       Alpha-D-glucose 1-phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00624}.
FT   BINDING      99     99       Alpha-D-glucose 1-phosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00624}.
FT   BINDING     164    164       Alpha-D-glucose 1-phosphate; via amide
FT                                nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00624}.
FT   BINDING     190    190       Alpha-D-glucose 1-phosphate; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00624}.
SQ   SEQUENCE   383 AA;  42866 MW;  F92E46E7AEE89EB2 CRC64;
     MKKEIVGMLL AGGEGKRLGQ LTRKLAKPAV YFGGKYRIID FPLSNCTNSG IDTVGVLTQY
     EPLALNGHIG IGSPWDLDRR HGGVTVLPPY IEKQGGSWYK GTADAIYQNR YYIEQYDPEY
     VLILSGDHIY KMDYDRMISH HKKLGADATI SVIEVPWEEA SRFGIMNTNE EMTITQFEEK
     PTTPISNLAS MGIYIFNWSV LKSYLIQDAK QANSSHDFGK DIIPKMLAKD LKLVAYPFEG
     YWKDVGTIKS YWEANMDLLD EHSSLMLNDP SWRIYSVNRN QPPQYISTRA YVRCSLVNEG
     CVVHGNVEQS ILFPGVHIGA NSSVFESVLM PNVKVGENVV LRRTIIMEGA CIPSGTHLAP
     SDPDDILVID KDTEFSPSIA ANQ
//
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