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Database: UniProt
Entry: Q2YB46
LinkDB: Q2YB46
Original site: Q2YB46 
ID   GLGC_NITMU              Reviewed;         425 AA.
AC   Q2YB46;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   29-MAY-2013, entry version 55.
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=Nmul_A0718;
OS   Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=323848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25196 / NCIMB 11849;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT   25196.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000103; ABB74025.1; -; Genomic_DNA.
DR   RefSeq; YP_411417.1; NC_007614.1.
DR   ProteinModelPortal; Q2YB46; -.
DR   SMR; Q2YB46; 13-418.
DR   STRING; 323848.Nmul_A0718; -.
DR   EnsemblBacteria; ABB74025; ABB74025; Nmul_A0718.
DR   GeneID; 3786064; -.
DR   KEGG; nmu:Nmul_A0718; -.
DR   PATRIC; 22724504; VBINitMul110821_0827.
DR   eggNOG; COG0448; -.
DR   HOGENOM; HOG000278607; -.
DR   KO; K00975; -.
DR   OMA; FCNINEA; -.
DR   ProtClustDB; PRK00725; -.
DR   BioCyc; NMUL323848:GKEC-735-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:EC.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
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    425       Glucose-1-phosphate adenylyltransferase.
FT                                /FTId=PRO_0000261883.
SQ   SEQUENCE   425 AA;  47822 MW;  AFF482127E5C7DD9 CRC64;
     MKLPADLRSY SQITRNSIAM ILAGGRGTRL RQLTDWRAKP AVPFGGKFRI IDFPLSNCVN
     SGIRRIGVAT QYKAQSLISH IQQGWGFLDG RFQEFIELLP AQQRTEESWY QGTADAVYQN
     IDILRSHNPD YVLILGGDHV YKMDYAKLLA DHIAKSAEMT IACIDLPLEE ASAFGVMSVT
     KDGRVTDFTE KPSVPTAVPG RPGYALVSMG IYVFNADFLF DQLIRDHDDP NSSHDFGKDL
     IPHLVPRSRV FTHRFSDSCV NMVSGVPYWR DVGTVEAYWE ANLDLVQVTP DLNLYDQDWP
     IWTHQEQLPP AKFVFDNDDR RGQALDSMVS GGCIISGATV RRSLLFSNVQ VRSYSVLEDS
     VILPNVDVGR NARLRRVVVD KNCIIPPGLE VGFDPVEDRK HFYVTETGVT LVTPEMLGQK
     IHYVR
//
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