GLGC_MYCS2
ID GLGC_MYCS2 Reviewed; 404 AA.
AC A0R2E1;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase {ECO:0000303|PubMed:27513637};
DE EC=2.7.7.27 {ECO:0000255|HAMAP-Rule:MF_00624};
DE AltName: Full=ADP-glucose pyrophosphorylase {ECO:0000303|PubMed:27513637};
DE AltName: Full=ADP-glucose synthase {ECO:0000255|HAMAP-Rule:MF_00624};
GN Name=glgC {ECO:0000303|PubMed:27513637};
GN OrderedLocusNames=MSMEG_5078 {ECO:0000312|EMBL:ABK75991.1},
GN MSMEI_4953 {ECO:0000312|EMBL:AFP41397.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27513637; DOI=10.1371/journal.ppat.1005768;
RA Koliwer-Brandl H., Syson K., van de Weerd R., Chandra G., Appelmelk B.,
RA Alber M., Ioerger T.R., Jacobs W.R. Jr., Geurtsen J., Bornemann S.,
RA Kalscheuer R.;
RT "Metabolic network for the biosynthesis of intra- and extracellular alpha-
RT glucans required for virulence of Mycobacterium tuberculosis.";
RL PLoS Pathog. 12:E1005768-E1005768(2016).
CC -!- FUNCTION: Involved in the biosynthesis of ADP-glucose building block,
CC required in the biosynthesis of maltose-1-phosphate (M1P) and in the
CC elongation reactions to produce linear alpha-1,4-glucans. Catalyzes the
CC reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce
CC pyrophosphate and ADP-Glc. {ECO:0000269|PubMed:27513637}.
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, ECO:0000255|RuleBase:RU003742}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of glgC shows a strong reduction in
CC alpha-glucan content. Combined inactivation of both glgC and treS
CC results in a complete absence of alpha-glucan.
CC {ECO:0000269|PubMed:27513637}.
CC -!- MISCELLANEOUS: Maltose-1-phosphate (M1P) is generated by two
CC alternative routes: the TreS-Pep2 branch and the GlgC-GlgM branch,
CC however it seems that the GlgC-GlgM branch provides most of M1P for the
CC GlgE pathway in M.smegmatis. {ECO:0000269|PubMed:27513637}.
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; CP000480; ABK75991.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP41397.1; -; Genomic_DNA.
DR RefSeq; WP_011730299.1; NZ_SIJM01000019.1.
DR RefSeq; YP_889329.1; NC_008596.1.
DR AlphaFoldDB; A0R2E1; -.
DR SMR; A0R2E1; -.
DR STRING; 246196.MSMEI_4953; -.
DR PRIDE; A0R2E1; -.
DR EnsemblBacteria; ABK75991; ABK75991; MSMEG_5078.
DR EnsemblBacteria; AFP41397; AFP41397; MSMEI_4953.
DR GeneID; 66736399; -.
DR KEGG; msg:MSMEI_4953; -.
DR KEGG; msm:MSMEG_5078; -.
DR PATRIC; fig|246196.19.peg.4957; -.
DR eggNOG; COG0448; Bacteria.
DR OMA; QEWDVDE; -.
DR OrthoDB; 1557977at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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..404
FT /note="Glucose-1-phosphate adenylyltransferase"
FT /id="PRO_0000438835"
FT BINDING 99
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT BINDING 164
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT BINDING 179..180
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT BINDING 197
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
SQ SEQUENCE 404 AA; 43908 MW; 58CA1249243A5466 CRC64;
MRELPHVLGI VLAGGEGKRL YPLTADRAKP AVPFGGAYRL IDFVLSNLVN ARYLRICVLT
QYKSHSLDRH ISQNWRLSGL AGEYITPVPA QQRLGPRWYT GSADAIYQSL NLIYDEDPDY
IIIFGADHVY RMDPEQMMQF HIESGAGATV AGIRVPRSEA SAFGCIDADE SGRIREFIEK
PADPPGTPDD PEQTFVSMGN YIFTTKVLID AIRADADDDH SDHDMGGDII PRLVADGMAA
VYDFKNNEVP GATERDHGYW RDVGTLDAFY DAHMDLVSVH PVFNLYNKRW PIRGESENLA
PAKFVNGGSA QESVVGAGSI ISAASVRNSV LSSNVVVDDG AIVEGSVLMP GVRIGRGAVV
RHAILDKNVV VGPGEMVGVD LDKDRERFAI SAGGVVAVGK GVWI
