GLGC2_VIBCH
ID GLGC2_VIBCH Reviewed; 407 AA.
AC Q9KLP4;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=VC_A0699;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003853; AAF96598.1; -; Genomic_DNA.
DR PIR; C82428; C82428.
DR RefSeq; NP_233086.1; NC_002506.1.
DR RefSeq; WP_001154339.1; NZ_LT906615.1.
DR AlphaFoldDB; Q9KLP4; -.
DR SMR; Q9KLP4; -.
DR STRING; 243277.VC_A0699; -.
DR PRIDE; Q9KLP4; -.
DR DNASU; 2612101; -.
DR EnsemblBacteria; AAF96598; AAF96598; VC_A0699.
DR GeneID; 57742088; -.
DR KEGG; vch:VC_A0699; -.
DR PATRIC; fig|243277.26.peg.3323; -.
DR eggNOG; COG0448; Bacteria.
DR HOGENOM; CLU_029499_14_1_6; -.
DR OMA; QKHLRDG; -.
DR BioCyc; VCHO:VCA0699-MON; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000584; 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..407
FT /note="Glucose-1-phosphate adenylyltransferase 2"
FT /id="PRO_0000195344"
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 407 AA; 45372 MW; 4F4C0797FF47AEAE CRC64;
MQDTLAVILA GGMGSRLSPL TDDRAKPAVP FGGKYRIIDF TLTNCLHSGL RRILVLTQYK
SHSLHKHLRN GWSIFNPELG EFITVVPPQM RKGGKWYEGT ADALFHNMWL LARSDAKYVV
VLSGDHIYRM DYAAMLEEHI SKNATLTIAC MQVPRHEASA FGVMAIDDDS RITCFVEKPA
DPPCIPNRPD HSLASMGIYI FNMDVLKKAL TEDAEIEQSS HDFGKDVIPK LIATGSVFAY
SFCSGKGRVA RDCYWRDVGT IDSFYDANMD LLQPVPPMNL YQKNWAIRTY EQQYPPARTV
SSATGNEGIF INSIIANGVI NSGGSVQHSI ISSNVRINDS ALIVDSILFD DVEVGEGCKL
IHCIIDKHVK IPPYTEIGLN PIEDRKRFHI SERGVVVVPE SYQFSTE
