GLGC_RUMCH
ID GLGC_RUMCH Reviewed; 426 AA.
AC Q9L385; B8I1Q4;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00624};
DE EC=2.7.7.27 {ECO:0000255|HAMAP-Rule:MF_00624};
DE AltName: Full=ADP-glucose pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00624};
DE Short=ADPGlc PPase {ECO:0000255|HAMAP-Rule:MF_00624};
DE AltName: Full=ADP-glucose synthase {ECO:0000255|HAMAP-Rule:MF_00624};
GN Name=glgC {ECO:0000255|HAMAP-Rule:MF_00624}; OrderedLocusNames=Ccel_3401;
OS Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 /
OS H10) (Clostridium cellulolyticum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminiclostridium.
OX NCBI_TaxID=394503;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10972834; DOI=10.1046/j.1365-2958.2000.02071.x;
RA Ravagnani A., Jennert K.C., Steiner E., Grunberg R., Jefferies J.R.,
RA Wilkinson S.R., Young D.I., Tidswell E.C., Brown D.P., Youngman P.J.,
RA Morris J.G., Young M.;
RT "Spo0A directly controls the switch from acid to solvent production in
RT solvent-forming clostridia.";
RL Mol. Microbiol. 37:1172-1185(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Zhou J., Richardson P.;
RT "Complete sequence of Clostridium cellulolyticum H10.";
RL Submitted (JAN-2009) 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:0000255|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:0000255|HAMAP-
CC Rule:MF_00624};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00624}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00624}.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000255|HAMAP-Rule:MF_00624}.
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DR EMBL; AJ277601; CAB89282.1; -; Genomic_DNA.
DR EMBL; CP001348; ACL77689.1; -; Genomic_DNA.
DR RefSeq; WP_015926741.1; NC_011898.1.
DR AlphaFoldDB; Q9L385; -.
DR SMR; Q9L385; -.
DR STRING; 394503.Ccel_3401; -.
DR EnsemblBacteria; ACL77689; ACL77689; Ccel_3401.
DR KEGG; cce:Ccel_3401; -.
DR eggNOG; COG0448; Bacteria.
DR HOGENOM; CLU_029499_14_0_9; -.
DR OMA; QEWDVDE; -.
DR OrthoDB; 1557977at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001349; 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 Gene3D; 3.90.550.10; -; 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 PANTHER; PTHR43523; PTHR43523; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR02091; glgC; 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; Carbohydrate metabolism; Glycogen biosynthesis;
KW Glycogen metabolism; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..426
FT /note="Glucose-1-phosphate adenylyltransferase"
FT /id="PRO_0000195288"
FT BINDING 165
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT BINDING 180..181
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT BINDING 191
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT CONFLICT 82
FT /note="D -> E (in Ref. 1; CAB89282)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="N -> S (in Ref. 1; CAB89282)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="A -> P (in Ref. 1; CAB89282)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 47081 MW; F20940BFD846231A CRC64;
MIRKEMIAML LAGGQGSRLG VLTKNVAKPA VLYGGKYRII DFSLSNCTNS GIDTVGVLTQ
YQPLKLNAHI GIGKPWDMDR IDGGVTILSP YLKAEMGEWF KGTANAVYQN IQYIDKYSPH
YVIILSGDHI YKMDYSKMLD FHKENHADAT ISVINVPYEE ASRYGIMNCH ENGKIYEFEE
KPKNPKSTLA SMGVYIFTWS TLREYLIKDN ECSDSVNDFG KNIIPAMLGD GKSMWAYQYS
GYWRDVGTIQ AFWESNMDLV SRVPQFNLFD PEWRIYTPNP VKPAHYIASS ACVKKSIIAE
GCSVHGTVIN SILFPGAYIE EGAVIQDSII MSNSRVCKNA YINRSIISEQ AIIGEKARLG
EGPDVPNEYK PGIYDSGITV VGEKSSIPAD AVIGKNVMID IGASAVDFTS LNVQSGKSVF
KGGVAE
