GLGC_MYCTU
ID GLGC_MYCTU Reviewed; 404 AA.
AC P9WN43; L0T8Q8; O05314; P64241;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
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 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:0000303|PubMed:18808383}; OrderedLocusNames=Rv1213;
GN ORFNames=MTCI364.25;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18808383; DOI=10.1111/j.1365-2958.2008.06445.x;
RA Sambou T., Dinadayala P., Stadthagen G., Barilone N., Bordat Y.,
RA Constant P., Levillain F., Neyrolles O., Gicquel B., Lemassu A., Daffe M.,
RA Jackson M.;
RT "Capsular glucan and intracellular glycogen of Mycobacterium tuberculosis:
RT biosynthesis and impact on the persistence in mice.";
RL Mol. Microbiol. 70:762-774(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
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:18808383,
CC 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:0000269|PubMed:18808383, ECO:0000269|PubMed:27513637}.
CC -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC {ECO:0000269|PubMed:18808383, ECO:0000269|PubMed:27513637}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of glgC reduces by half the
CC extracellular (capsular) alpha-D-glucan and intracellular glycogen
CC contents (PubMed:18808383, PubMed:27513637). Cells lacking this gene
CC are not affected in their multiplication or persistence in the BALB/c
CC mouse infection model (PubMed:18808383). Combined inactivation of both
CC glgC and treS results in a complete absence of maltose-1-phosphate
CC (M1P) and alpha-glucan, whereas combined inactivation of both glgC and
CC otsA results only in a complete absence of alpha-glucan
CC (PubMed:27513637). {ECO:0000269|PubMed:18808383,
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 TreS-Pep2 branch provides most of M1P for the
CC GlgE pathway in M.tuberculosis. {ECO:0000269|PubMed:27513637}.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43969.1; -; Genomic_DNA.
DR PIR; C70610; C70610.
DR RefSeq; NP_215729.1; NC_000962.3.
DR RefSeq; WP_003406249.1; NZ_NVQJ01000039.1.
DR AlphaFoldDB; P9WN43; -.
DR SMR; P9WN43; -.
DR STRING; 83332.Rv1213; -.
DR PaxDb; P9WN43; -.
DR DNASU; 887933; -.
DR GeneID; 45425183; -.
DR GeneID; 887933; -.
DR KEGG; mtu:Rv1213; -.
DR TubercuList; Rv1213; -.
DR eggNOG; COG0448; Bacteria.
DR OMA; QEWDVDE; -.
DR PhylomeDB; P9WN43; -.
DR BioCyc; MetaCyc:G185E-5383-MON; -.
DR UniPathway; UPA00164; -.
DR UniPathway; UPA00934; -.
DR PHI-base; PHI:6731; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
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:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009250; P:glucan biosynthetic process; IMP:MTBBASE.
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 1: Evidence at protein level;
KW ATP-binding; Capsule biogenesis/degradation; Carbohydrate metabolism;
KW Glycogen biosynthesis; Glycogen metabolism; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..404
FT /note="Glucose-1-phosphate adenylyltransferase"
FT /id="PRO_0000195309"
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; 43800 MW; D1D7C8934A8CC5D2 CRC64;
MREVPHVLGI VLAGGEGKRL YPLTADRAKP AVPFGGAYRL IDFVLSNLVN ARYLRICVLT
QYKSHSLDRH ISQNWRLSGL AGEYITPVPA QQRLGPRWYT GSADAIYQSL NLIYDEDPDY
IVVFGADHVY RMDPEQMVRF HIDSGAGATV AGIRVPRENA TAFGCIDADD SGRIRSFVEK
PLEPPGTPDD PDTTFVSMGN YIFTTKVLID AIRADADDDH SDHDMGGDIV PRLVADGMAA
VYDFSDNEVP GATDRDRAYW RDVGTLDAFY DAHMDLVSVH PVFNLYNKRW PIRGESENLA
PAKFVNGGSA QESVVGAGSI ISAASVRNSV LSSNVVVDDG AIVEGSVIMP GTRVGRGAVV
RHAILDKNVV VGPGEMVGVD LEKDRERFAI SAGGVVAVGK GVWI
