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 01-MAY-2013, entry version 70.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase;
DE EC=2.7.7.27;
DE AltName: Full=ADP-glucose pyrophosphorylase;
DE Short=ADPGlc PPase;
DE AltName: Full=ADP-glucose synthase;
GN Name=glgC; 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: Catalyzes the synthesis of ADP-glucose, a sugar donor
CC used in elongation reactions on alpha-glucans (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + alpha-D-glucose 1-phosphate =
CC diphosphate + ADP-glucose.
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family.
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DR EMBL; BA000004; BAB04806.1; -; Genomic_DNA.
DR PIR; G83785; G83785.
DR RefSeq; NP_241953.1; NC_002570.2.
DR ProteinModelPortal; Q9KDX4; -.
DR STRING; 272558.BH1087; -.
DR DNASU; 892001; -.
DR EnsemblBacteria; BAB04806; BAB04806; BAB04806.
DR GeneID; 892001; -.
DR KEGG; bha:BH1087; -.
DR PATRIC; 18939232; VBIBacHal18977_1134.
DR eggNOG; COG0448; -.
DR HOGENOM; HOG000278603; -.
DR KO; K00975; -.
DR OMA; YTRPRYL; -.
DR ProtClustDB; PRK05293; -.
DR BioCyc; BHAL272558:GJC5-1165-MONOMER; -.
DR UniPathway; UPA00164; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IEA:HAMAP.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:HAMAP.
DR HAMAP; MF_00624; GlgC; 1; -.
DR InterPro; IPR005836; ADP_Glu_pyroP_CS.
DR InterPro; IPR011831; GlgC.
DR InterPro; IPR023049; GlgC_bac.
DR InterPro; IPR005835; NTP_transferase.
DR InterPro; IPR011004; Trimer_LpxA-like.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF51161; Trimer_LpxA_like; 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;
KW ATP-binding; Carbohydrate metabolism; Complete proteome;
KW Glycogen biosynthesis; Glycogen metabolism; Nucleotide-binding;
KW Nucleotidyltransferase; Transferase.
FT CHAIN 1 383 Glucose-1-phosphate adenylyltransferase.
FT /FTId=PRO_0000195280.
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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