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Database: UniProt
Entry: A4BPW1_9GAMM
LinkDB: A4BPW1_9GAMM
Original site: A4BPW1_9GAMM 
ID   A4BPW1_9GAMM            Unreviewed;       422 AA.
AC   A4BPW1;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 86.
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=NB231_04385 {ECO:0000313|EMBL:EAR22116.1};
OS   Nitrococcus mobilis Nb-231.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Nitrococcus.
OX   NCBI_TaxID=314278 {ECO:0000313|EMBL:EAR22116.1, ECO:0000313|Proteomes:UP000003374};
RN   [1] {ECO:0000313|EMBL:EAR22116.1, ECO:0000313|Proteomes:UP000003374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nb-231 {ECO:0000313|EMBL:EAR22116.1,
RC   ECO:0000313|Proteomes:UP000003374};
RA   Waterbury J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA   Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) 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: 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:EAR22116.1}.
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DR   EMBL; AAOF01000004; EAR22116.1; -; Genomic_DNA.
DR   RefSeq; WP_005000061.1; NZ_CH672427.1.
DR   AlphaFoldDB; A4BPW1; -.
DR   STRING; 314278.NB231_04385; -.
DR   eggNOG; COG0448; Bacteria.
DR   HOGENOM; CLU_029499_14_1_6; -.
DR   OrthoDB; 9801810at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000003374; 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; 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:UP000003374};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00624}.
FT   DOMAIN          19..282
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   BINDING         176
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00624"
FT   BINDING         191..192
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00624"
FT   BINDING         209
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00624"
FT   SITE            71
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            110
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   422 AA;  47387 MW;  3D69F1C5E2203272 CRC64;
     MYFERNPRFV SRLTRDTLAI ILAGGRGGRL ANLTDWRTKP ALPFGGKFRL IDFPLSNCIN
     SGVRRIQIVT QYKAHSLIQH VQRGWGFLRG EFGEFVEIVP AQQRLDKPLW FAGTADAIHQ
     NIDIIKAHRP RYVLILAGDH VYKMDYGPMI ALHVEHAADM TVGCVEMARE RARAFGVMTV
     DENGRVLRFT EKPQEPNPVP GKPDTALVSM GIYVFEREYL FEQLRADAEN IDSSRDFGRD
     VIPAAIAHNK VIAYPFADPK SGEQPYWRDV GTVDAFFEAN LELIGKGSEL DLYDQDRPIW
     TYQAQLPPAK FINDAGHRGI AIDSMVSGGD IIQGAEVRHS LLFSQVLVRP RAKIQDAVIL
     PDVVVGEGCR IRRCVIDEGC RIPRETVIGE DDVADRERFF VSPKGVVLVT AEMLGQEVAH
     VR
//
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