GLGC2_VIBPA
ID GLGC2_VIBPA Reviewed; 404 AA.
AC Q87HX3;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00624};
DE EC=2.7.7.27 {ECO:0000255|HAMAP-Rule:MF_00624};
DE AltName: Full=ADP-glucose pyrophosphorylase 2 {ECO:0000255|HAMAP-Rule:MF_00624};
DE Short=ADPGlc PPase 2 {ECO:0000255|HAMAP-Rule:MF_00624};
DE AltName: Full=ADP-glucose synthase 2 {ECO:0000255|HAMAP-Rule:MF_00624};
GN Name=glgC2 {ECO:0000255|HAMAP-Rule:MF_00624}; OrderedLocusNames=VPA0833;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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}.
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DR EMBL; BA000032; BAC62176.1; -; Genomic_DNA.
DR RefSeq; NP_800343.1; NC_004605.1.
DR RefSeq; WP_005454156.1; NC_004605.1.
DR AlphaFoldDB; Q87HX3; -.
DR SMR; Q87HX3; -.
DR STRING; 223926.28809068; -.
DR EnsemblBacteria; BAC62176; BAC62176; BAC62176.
DR GeneID; 1191522; -.
DR KEGG; vpa:VPA0833; -.
DR PATRIC; fig|223926.6.peg.3763; -.
DR eggNOG; COG0448; Bacteria.
DR HOGENOM; CLU_029499_14_1_6; -.
DR OMA; QKHLRDG; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000002493; Chromosome 2.
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..404
FT /note="Glucose-1-phosphate adenylyltransferase 2"
FT /id="PRO_0000195347"
FT BINDING 97
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT BINDING 162
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT BINDING 177..178
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT BINDING 195
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
SQ SEQUENCE 404 AA; 44614 MW; 8FEF2F7E949E96F3 CRC64;
MQDALAVILA GGMGSRLSPL TDDRAKPAVP FGGKYRIIDF TLTNCLNSGL RKILVLTQYK
SHSLQKHLRD GWSIFNPELG EYITAVPPQM RKGGAWYEGT ADAIYHNLWL LSRNDAKYVV
VLSGDHIYRM DYAAMLEEHK EKGAKLTVAC MDVPVKDASA FGVMGIAENG LVKSFVEKPE
NPPTLPDDNA KSLASMGIYI FDMDVLKEAL TEDAKLETSS HDFGNDIIPK LIDTESVYAY
KFCGSKGRVD KDCYWRDVGT IDSFYEANMD LLEPVPPMNL YQSNWAIRTY EPQFPPARTV
SSATGNEGIF INSIIATGVI NSGGSVQHSI ISSNVRIQDS ATVVDSIIFD DVEVGEGSQL
VNCIVDKHVR IPPNTQIGIN KVEDAKRFKI SEKGIVVIPE SYQF
