ID A0A143BNE9_9BACT Unreviewed; 420 AA.
AC A0A143BNE9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00624};
DE EC=2.7.7.27 {ECO:0000256|HAMAP-Rule:MF_00624};
DE AltName: Full=ADP-glucose pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00624};
DE Short=ADPGlc PPase {ECO:0000256|HAMAP-Rule:MF_00624};
DE AltName: Full=ADP-glucose synthase {ECO:0000256|HAMAP-Rule:MF_00624};
GN Name=glgC {ECO:0000256|HAMAP-Rule:MF_00624};
GN ORFNames=GEMMAAP_16465 {ECO:0000313|EMBL:AMW05954.1};
OS Gemmatimonas phototrophica.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=1379270 {ECO:0000313|EMBL:AMW05954.1, ECO:0000313|Proteomes:UP000076404};
RN [1] {ECO:0000313|EMBL:AMW05954.1, ECO:0000313|Proteomes:UP000076404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP64 {ECO:0000313|EMBL:AMW05954.1,
RC ECO:0000313|Proteomes:UP000076404};
RX PubMed=24821787; DOI=10.1073/pnas.1400295111;
RA Zeng Y., Feng F., Medova H., Dean J., Koblizek M.;
RT "Functional type 2 photosynthetic reaction centers found in the rare
RT bacterial phylum Gemmatimonadetes.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:7795-7800(2014).
RN [2] {ECO:0000313|EMBL:AMW05954.1, ECO:0000313|Proteomes:UP000076404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP64 {ECO:0000313|EMBL:AMW05954.1,
RC ECO:0000313|Proteomes:UP000076404};
RX PubMed=26636755; DOI=10.1111/1758-2229.12363;
RA Zeng Y., Baumbach J., Barbosa E.G., Azevedo V., Zhang C., Koblizek M.;
RT "Metagenomic evidence for the presence of phototrophic Gemmatimonadetes
RT bacteria in diverse environments.";
RL Environ. Microbiol. Rep. 8:139-149(2016).
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:0000256|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:0000256|HAMAP-
CC Rule:MF_00624};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00624}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00624}.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000256|ARBA:ARBA00010443,
CC ECO:0000256|HAMAP-Rule:MF_00624}.
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DR EMBL; CP011454; AMW05954.1; -; Genomic_DNA.
DR RefSeq; WP_026848315.1; NZ_CP011454.1.
DR AlphaFoldDB; A0A143BNE9; -.
DR STRING; 1379270.GEMMAAP_16465; -.
DR GeneID; 78445706; -.
DR KEGG; gph:GEMMAAP_16465; -.
DR eggNOG; COG0448; Bacteria.
DR OrthoDB; 9801810at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000076404; 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 CDD; cd02508; ADP_Glucose_PP; 1.
DR CDD; cd04651; LbH_G1P_AT_C; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 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 NCBIfam; TIGR02091; glgC; 1.
DR PANTHER; PTHR43523:SF2; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE; 1.
DR PANTHER; PTHR43523; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE-RELATED; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00624};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_00624};
KW Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056, ECO:0000256|HAMAP-
KW Rule:MF_00624};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600, ECO:0000256|HAMAP-
KW Rule:MF_00624};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00624};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00624}; Reference proteome {ECO:0000313|Proteomes:UP000076404};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00624}.
FT DOMAIN 16..284
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT BINDING 107
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00624"
FT BINDING 172
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00624"
FT BINDING 187..188
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00624"
FT BINDING 205
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00624"
FT SITE 67
FT /note="Could play a key role in the communication between
FT the regulatory and the substrate sites"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00624"
FT SITE 106
FT /note="Could play a key role in the communication between
FT the regulatory and the substrate sites"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00624"
SQ SEQUENCE 420 AA; 46751 MW; F6AE3DA9B0AA0CC0 CRC64;
MTPYTRGTLS RHAMAYVLAG GRGSRLYELT DRRAKPAVYF GGKTRIIDFA LSNAINSGIR
RIGVATQYKA HSLIRHLQRG WNFLRPERNE SFDILPASQR VSETQWYEGT ADAVYQNLDI
IEAYHPEYMV ILAGDHIYKM DYELMLQQHV AQGADVTVGV LEVPRMEATG FGVMHVDEHD
RIVHFLEKPA DPPGIPGNPD MALASMGIYV FKTSFLADLL RRDAVDPHTT HDFGKDLIPY
VVANGKAVAH RFSDSCVKAS RESEAYWRDV GTIDAYWEAN IDLTSVLPGL DMYDHDWPIW
TYGEITPPAK FVHAEEGRRG FALDSLISGG CIVSGAAVFR SLMFTNVRIH SYAHLDGAVL
QPDVDVGRGA RLTNVVVDRG VRIPPGLIVG EDPALDGARF RRSDKGVVLI TQPMIDRLSL
//
