GenomeNet

Database: UniProt
Entry: Q9RNH7
LinkDB: Q9RNH7
Original site: Q9RNH7 
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   03-SEP-2014, entry version 80.
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF181035; AAD53958.1; -; Genomic_DNA.
DR   EMBL; CP000143; ABA79047.1; -; Genomic_DNA.
DR   EMBL; AF095720; AAC64193.1; -; Genomic_DNA.
DR   RefSeq; WP_002720043.1; NZ_AKVW01000001.1.
DR   RefSeq; YP_352948.1; NC_007493.2.
DR   ProteinModelPortal; Q9RNH7; -.
DR   SMR; Q9RNH7; 9-416.
DR   STRING; 272943.RSP_2886; -.
DR   EnsemblBacteria; ABA79047; ABA79047; 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; MLAYHVE; -.
DR   OrthoDB; EOG6W9X86; -.
DR   PhylomeDB; Q9RNH7; -.
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:UniProtKB-EC.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.550.10; -; 2.
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; 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.
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
//
DBGET integrated database retrieval system