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Database: UniProt
Entry: J4TFP0_9FIRM
LinkDB: J4TFP0_9FIRM
Original site: J4TFP0_9FIRM 
ID   J4TFP0_9FIRM            Unreviewed;       381 AA.
AC   J4TFP0;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
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   ECO:0000313|EMBL:EJP21704.1};
GN   ORFNames=HMPREF1142_2133 {ECO:0000313|EMBL:EJP21704.1};
OS   Peptostreptococcaceae bacterium AS15.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae.
OX   NCBI_TaxID=936556 {ECO:0000313|EMBL:EJP21704.1, ECO:0000313|Proteomes:UP000006605};
RN   [1] {ECO:0000313|EMBL:EJP21704.1, ECO:0000313|Proteomes:UP000006605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS15 {ECO:0000313|EMBL:EJP21704.1,
RC   ECO:0000313|Proteomes:UP000006605};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJP21704.1}.
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DR   EMBL; ALJM01000033; EJP21704.1; -; Genomic_DNA.
DR   AlphaFoldDB; J4TFP0; -.
DR   PATRIC; fig|936556.4.peg.1452; -.
DR   OrthoDB; 9803871at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000006605; Unassembled WGS sequence.
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; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00624};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00624};
KW   Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056, ECO:0000256|HAMAP-
KW   Rule:MF_00624}; Glycogen metabolism {ECO:0000256|HAMAP-Rule:MF_00624};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00624};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00624,
KW   ECO:0000313|EMBL:EJP21704.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006605};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00624}.
FT   DOMAIN          8..260
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   BINDING         100
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00624"
FT   BINDING         165
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00624"
FT   BINDING         180..181
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00624"
FT   BINDING         191
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00624"
FT   SITE            60
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            99
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   381 AA;  42780 MW;  E558CA0D9CD08908 CRC64;
     MNKKEMIAMI LAGGQGSRLK MFTENLAKPA VPFGAKYRVI DFVISNCANS GIDTVGILTQ
     YKPFELHNHI GIGASWGLNR RDGGAYILPP YMSEKEQNFY KGTAHAIEQN KEFIDSFNPE
     YLLVLSGDHI YKMNYKKMLD LHKKNKADAT IAVIEVPWEE APRFGIMNTN EDGSIYEFEE
     KPENPKSNLA SMGIYIFNWA LLRKEFEVCE TEGRPKVDFG QDIIPSLLGQ GKRLFSYKFK
     GYWKDVGTLS SYWESNMDLL DMDNQLNLFD SSWQIRSHNK SLPPLYISKD AILDNSIVSD
     GAIIKGVVRN SVISSSVEVE EGAIVEDSVI MSNTFVGKNA RVIKSIIGEN VMIHEGVHVC
     DKDGGLYSVG NNMELRGEIS E
//
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