GLGC_BACCL
ID GLGC_BACCL Reviewed; 250 AA.
AC P30522;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 25-MAY-2022, entry version 64.
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;
DE Flags: Fragment;
GN Name=glgC;
OS Bacillus caldolyticus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=1394;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1296817; DOI=10.3109/10425179209034021;
RA Kiel J.A.K.W., Boels J.M., Beldman G., Venema G.;
RT "The glgB gene from the thermophile Bacillus caldolyticus encodes a
RT thermolabile branching enzyme.";
RL DNA Seq. 3:221-232(1992).
CC -!- FUNCTION: Catalyzes the synthesis of ADP-glucose, a sugar donor used in
CC elongation reactions on alpha-glucans. {ECO:0000250}.
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;
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000305}.
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DR EMBL; Z14057; CAA78441.1; -; Genomic_DNA.
DR PIR; C56639; C56639.
DR AlphaFoldDB; P30522; -.
DR SMR; P30522; -.
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; -; 1.
DR InterPro; IPR011831; ADP-Glc_PPase.
DR InterPro; IPR005836; ADP_Glu_pyroP_CS.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43523; PTHR43523; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; SSF53448; 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; Glycogen biosynthesis;
KW Glycogen metabolism; Nucleotide-binding; Nucleotidyltransferase;
KW Transferase.
FT CHAIN 1..>250
FT /note="Glucose-1-phosphate adenylyltransferase"
FT /id="PRO_0000195277"
FT NON_TER 250
SQ SEQUENCE 250 AA; 28215 MW; A5ADBA087EB873F7 CRC64;
MKKKCIAMLL AGGQGSRLRS LTKNIAKPAV PFGGKYRIID FTLSNCTNSG IDTVGVLTQY
QPLLLHSYIG IGSAWDLDRR NGGVTVLPPY SASSGVKWYE GTANAIYQNM NYIEQYDPDY
VLVLSGDHIY KMDYQQMLDY HIAKQADATI SVIEVPWEEA SRFGIMNTNE NMEIVEFAEK
PANPKSNLAS MGIYIFNWPL LREYLQIDNA DPHSSHDFGK DVIPRLLREN KRLVAYPFKG
YWKDVGTVKS