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Database: UniProt
Entry: A0A0V8HNX9_9BACI
LinkDB: A0A0V8HNX9_9BACI
Original site: A0A0V8HNX9_9BACI 
ID   A0A0V8HNX9_9BACI        Unreviewed;       385 AA.
AC   A0A0V8HNX9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=GA0061094_1588 {ECO:0000313|EMBL:SCB94664.1};
OS   [Bacillus] enclensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX   NCBI_TaxID=1402860 {ECO:0000313|EMBL:SCB94664.1, ECO:0000313|Proteomes:UP000181997};
RN   [1] {ECO:0000313|EMBL:SCB94664.1, ECO:0000313|Proteomes:UP000181997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SGD-1123 {ECO:0000313|EMBL:SCB94664.1,
RC   ECO:0000313|Proteomes:UP000181997};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) 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}.
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DR   EMBL; FMAU01000001; SCB94664.1; -; Genomic_DNA.
DR   RefSeq; WP_032087242.1; NZ_KQ758482.1.
DR   AlphaFoldDB; A0A0V8HNX9; -.
DR   OrthoDB; 9801810at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000181997; 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; 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};
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   385 AA;  43085 MW;  6A85DD57E3940CD3 CRC64;
     MAKGRCVAML LAGGKGSRLS SLTKNLAKPA VPFGGKYRII DFTLSNCTNS GIDTVGVLTQ
     YQPLVLNSYI GIGSAWDLDR KNGGVTVLPP YAESSEMRWY TGTASAIYQN MNYLEQYDPE
     YVLVLSGDHI YKMDYSKMLD YHIEKKADVS ISVIEVDWSE ASRFGLMNTN EEMRITEFEE
     KPAYPKSNLA SMGIYIFNWS VLKDFLEMDE RNPHSSHDFG KDVIPLLLDE KKKLMAYPFK
     GYWKDVGTVK SLWEANMDLI DEDNELNLFD HEWRVYSVNP NEPPQYISAD ALVEGSLVNE
     GCTIEGTISK SVLFQGTTVK KGAHVSRSVI MPDALIGENS YIEQAIVPPN VKVPSGVCIM
     PEEGSDEVIL VTEAFIDTLL EQEEV
//
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