GLGC_CERS4
ID GLGC_CERS4 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-AUG-2022, entry version 110.
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};
GN OrderedLocusNames=RHOS4_14790, RSP_2886;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
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 pyrophosphorylase
RT 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 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
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., 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: Involved in the biosynthesis of ADP-glucose, a building block
CC required for the elongation reactions to produce glycogen. Catalyzes
CC the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to
CC produce pyrophosphate and ADP-Glc. {ECO:0000255|HAMAP-Rule:MF_00624}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose
CC + diphosphate; Xref=Rhea:RHEA:12120, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57498,
CC ChEBI:CHEBI:58601; EC=2.7.7.27; Evidence={ECO:0000255|HAMAP-
CC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) 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_CP030271.1.
DR RefSeq; YP_352948.1; NC_007493.2.
DR AlphaFoldDB; Q9RNH7; -.
DR SMR; Q9RNH7; -.
DR STRING; 272943.RSP_2886; -.
DR EnsemblBacteria; ABA79047; ABA79047; RSP_2886.
DR GeneID; 57470210; -.
DR KEGG; rsp:RSP_2886; -.
DR PATRIC; fig|272943.9.peg.1822; -.
DR eggNOG; COG0448; Bacteria.
DR OMA; QEWDVDE; -.
DR PhylomeDB; Q9RNH7; -.
DR BRENDA; 2.7.7.27; 5383.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000002703; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniRule.
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_sf.
DR PANTHER; PTHR43523; PTHR43523; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
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; Glycogen biosynthesis;
KW Glycogen metabolism; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..423
FT /note="Glucose-1-phosphate adenylyltransferase"
FT /id="PRO_0000195323"
FT BINDING 107
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT BINDING 172
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT BINDING 187..188
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT BINDING 205
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT CONFLICT 196
FT /note="P -> T (in Ref. 3; AAC64193)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="D -> K (in Ref. 3; AAC64193)"
FT /evidence="ECO:0000305"
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
