GLGC_YERPE
ID GLGC_YERPE Reviewed; 476 AA.
AC Q8ZA77; Q0WA77;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=YPO3940, y3888, YP_3302;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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; AL590842; CAL22521.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM87433.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS63467.1; -; Genomic_DNA.
DR PIR; AF0479; AF0479.
DR RefSeq; YP_002348811.1; NC_003143.1.
DR AlphaFoldDB; Q8ZA77; -.
DR SMR; Q8ZA77; -.
DR IntAct; Q8ZA77; 1.
DR STRING; 214092.YPO3940; -.
DR PaxDb; Q8ZA77; -.
DR DNASU; 1148835; -.
DR EnsemblBacteria; AAM87433; AAM87433; y3888.
DR EnsemblBacteria; AAS63467; AAS63467; YP_3302.
DR KEGG; ype:YPO3940; -.
DR KEGG; ypj:CH55_2619; -.
DR KEGG; ypk:y3888; -.
DR KEGG; ypl:CH46_1118; -.
DR KEGG; ypm:YP_3302; -.
DR KEGG; ypv:BZ15_3765; -.
DR KEGG; ypw:CH59_1887; -.
DR PATRIC; fig|214092.21.peg.4466; -.
DR eggNOG; COG0448; Bacteria.
DR HOGENOM; CLU_029499_14_1_6; -.
DR OMA; QEWDVDE; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
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.
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 Reference proteome; Transferase.
FT CHAIN 1..476
FT /note="Glucose-1-phosphate adenylyltransferase"
FT /id="PRO_0000195352"
FT BINDING 114
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT BINDING 179
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT BINDING 194..195
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT BINDING 212
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
SQ SEQUENCE 476 AA; 53114 MW; BADCE7F3D7313046 CRC64;
MVRFESTDSL MLARQLPNKT VALILAGGRG SRLKDLTATR AKPAVHFGGK FRIIDFALSN
CLNSGVRRIG VITQYQSHTL VQHIQRGWSF LNEEMNEFVD LLPAQQRLST EQWYKGTADA
VCQNLDIIRR YDAEYIVILA GDHIYKMDYS RMLLDHVEKG AECTVACIPV PISEGSEFGI
MEVTADYQIT AFYEKPANPP PIPGDPSNAL ASMGIYIFNA DYLFKLLEED NNTPGSSHDF
GKDIIPQLTA RKVVWAHPFD LSCVTSNAEL PPYWRDVGTL DAYWRANLDL ASVTPELDMY
DRAWPIRTHM EPLPPAKFVQ DRSGSHGMTM NSLVSGGCIV SGSVVVHSVL FPRVRVNSFC
TIDSSLLLPD VHVGRSCRLR RCIIDRACHI PEGMVIGENA DEDSARFYRS EGGGGVSDSG
YAGKVRGKIE PLGFLFVRLD LLIRLSLLIR LNLFIRMNLL IILTLFFKLA SIQASH
