GLGC_ACIAC
ID GLGC_ACIAC Reviewed; 435 AA.
AC A1TRG1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Aave_2982;
OS Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=397945;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAC00-1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL Submitted (DEC-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: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; CP000512; ABM33549.1; -; Genomic_DNA.
DR RefSeq; WP_011796059.1; NC_008752.1.
DR AlphaFoldDB; A1TRG1; -.
DR SMR; A1TRG1; -.
DR STRING; 397945.Aave_2982; -.
DR PRIDE; A1TRG1; -.
DR EnsemblBacteria; ABM33549; ABM33549; Aave_2982.
DR KEGG; aav:Aave_2982; -.
DR eggNOG; COG0448; Bacteria.
DR HOGENOM; CLU_029499_14_4_4; -.
DR OMA; YRMDFSQ; -.
DR OrthoDB; 1557977at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000002596; 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 PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 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..435
FT /note="Glucose-1-phosphate adenylyltransferase"
FT /id="PRO_1000051554"
FT REGION 408..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 199
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
SQ SEQUENCE 435 AA; 48671 MW; 6E6E9630ED192184 CRC64;
MSSTKNVLAI VMAGGEGSRL HPLTAERCKP AVPFNGKHRI VDFVLSNLVN SEIYSIYLLV
QYKSQSLIEH IRQSWTMTRF IPQHFVTVVP PQMRNGPEWF QGTADSVYQN IHLIESFKPD
IVAVFGADHI YRMDVRQMID FHVKNDAHVS VATLPVKLAD CNQFGIVETD DNHRIVDFVE
KPQTPPRPMP GSSTHALASM GNYLFNADIL LDALREAHET GHSDFGKHIL PAMLKSHRLM
AYDFDTNTIP GTEPYEEHGY WRDVGTIDAY YQAHFDTLGA TPRFRMTNRH WPIYASPDQA
ESAQIENGVI HRSVVGSGSI VDGASLDNAM LRRSVVVERD ARLEHCIVME RSRIGRGAQV
RRAIIDQDND IPAHERIGFD LEADRKRFHV TASGIVVVPR QFFKPQSLQS TTPSIGRARP
SVASASEGSG LKVAA
