ID GLGC_RHOS4 Reviewed; 423 AA.
AC Q9RNH7; O87670; Q3J2D7;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 29-MAY-2013, entry version 72.
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=RHOS4_14790; ORFNames=RSP_2886;
OS Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM
OS 158).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Igarashi R.Y., Meyer C.R.;
RT "Cloning, sequencing, and expression of the ADP-glucose
RT pyrophosphorylase gene (glgC) from Rhodobacter sphaeroides 2.4.1.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J.,
RA Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-212.
RA Igarashi R.Y., Meyer C.R.;
RL Submitted (SEP-1998) 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; AF181035; AAD53958.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA79047.1; -; Genomic_DNA.
DR EMBL; AF095720; AAC64193.1; -; Genomic_DNA.
DR RefSeq; YP_352948.1; NC_007493.1.
DR ProteinModelPortal; Q9RNH7; -.
DR SMR; Q9RNH7; 9-416.
DR STRING; 272943.RSP_2886; -.
DR GeneID; 3720626; -.
DR KEGG; rsp:RSP_2886; -.
DR PATRIC; 23152871; VBIRhoSph57909_1822.
DR eggNOG; COG0448; -.
DR HOGENOM; HOG000278607; -.
DR KO; K00975; -.
DR OMA; SKNHIAP; -.
DR ProtClustDB; PRK00725; -.
DR BioCyc; RSPH272943:GJAS-1514-MONOMER; -.
DR BRENDA; 2.7.7.27; 5383.
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; FALSE_NEG.
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 1 423 Glucose-1-phosphate adenylyltransferase.
FT /FTId=PRO_0000195323.
FT CONFLICT 196 196 P -> T (in Ref. 3; AAC64193).
FT CONFLICT 212 212 D -> K (in Ref. 3; AAC64193).
SQ SEQUENCE 423 AA; 47311 MW; 921F2D33BC9807F1 CRC64;
MKAQPPLRLT AQAMAFVLAG GRGSRLKELT DRRAKPAVYF GGKARIIDFA LSNAMNSGIR
KMAIATQYKA HSLIRHIQRG WNFFREERNE YLDILPASQR VDENRWYLGT ADAVTQNIDI
VDSYDIKYVI ILAGDHVYKM DYEIMLRQHC ETGADVTIGC LTVPRAEATA FGVMHVDANL
RITDFLEKPA DPPGIPGDEA NALASMGIYV FDWAFLRDLL IRDAEDPNSS HDFGHDLIPA
IVKNGKAMAH RFSDSCVMTG LETEPYWRDV GTIDAFWQAN IDLTDFTPKL DLYDREWPIW
TYSQIVPPAK FIHDSENRRG TAISSLVSGD CIVSGSEIRS SLLFTGCRTH SYSSMSHVVA
LPHVTVNRKA DLTNCVLDRG VVVPEGLVIG QDAEEDARWF RRSEGGIVLV TQDMLDARAR
ALN
//