ID W4DRN5_9BACL Unreviewed; 407 AA.
AC W4DRN5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=C173_16356 {ECO:0000313|EMBL:ETT70266.1};
OS Paenibacillus sp. FSL R7-277.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1227352 {ECO:0000313|EMBL:ETT70266.1, ECO:0000313|Proteomes:UP000019051};
RN [1] {ECO:0000313|EMBL:ETT70266.1, ECO:0000313|Proteomes:UP000019051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R7-277 {ECO:0000313|EMBL:ETT70266.1,
RC ECO:0000313|Proteomes:UP000019051};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:ETT70266.1}.
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DR EMBL; ASPX01000054; ETT70266.1; -; Genomic_DNA.
DR RefSeq; WP_036726474.1; NZ_ASPX01000054.1.
DR AlphaFoldDB; W4DRN5; -.
DR PATRIC; fig|1227352.4.peg.3276; -.
DR eggNOG; COG0448; Bacteria.
DR OrthoDB; 9801810at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000019051; 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|HAMAP-Rule:MF_00624};
KW 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:ETT70266.1};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00624, ECO:0000313|EMBL:ETT70266.1}.
FT DOMAIN 8..260
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT BINDING 99
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00624"
FT BINDING 164
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00624"
FT BINDING 179..180
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00624"
FT BINDING 190
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"
SQ SEQUENCE 407 AA; 44982 MW; C42083111D382B19 CRC64;
MSKKECIAML LAGGEGRRLA PLTSSMAKPA VPFGGQYRII DFPLSNCVNS KIDTIGVLTQ
YEAESLHQHI GEGEPWGLHS RSDRGVRLLP SGIEGRDSYT GTADAIYKNI EYIDSQNPEH
VLILSGDHIY HMDYRKMLDY HIAKSAKATI SVMEVPWDEA SRFGVMNVDE DFKISEFAEK
PKAPKSNLAS MGIYLFEWAY LKAHLLRDAA NAESGHDFGK DVIPAMLDAS DELFAYRFEG
YWRDVGTVGS LWEAHMDLLQ EDGFQLDNSR WPMYSRAQRT KLAALRPRTQ QAASADCLIH
ETCQLEGSPQ RSVIFSGVEI GKQSRIKQSV VMPGARIGRG VLIEHAIIGE GAVIKDGAVI
KGSADNIVVV GPHEIVAAKP LVRTQPARLL QEVYEKAGRL RAEGMPS
//
