ID PHSG_MYCTU Reviewed; 863 AA.
AC P9WMW1; L0T6B6; Q10639;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Glycogen phosphorylase;
DE EC=2.4.1.1;
GN Name=glgP; OrderedLocusNames=Rv1328; ORFNames=MTCY130.13;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; 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 IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011445;
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).
CC -!- FUNCTION: Phosphorylase is an important allosteric enzyme in
CC carbohydrate metabolism. Enzymes from different sources differ in their
CC regulatory mechanisms and in their natural substrates. However, all
CC known phosphorylases share catalytic and structural properties (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-
CC glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732,
CC Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44086.1; -; Genomic_DNA.
DR PIR; D70770; D70770.
DR RefSeq; NP_215844.1; NC_000962.3.
DR RefSeq; WP_003901135.1; NZ_NVQJ01000031.1.
DR AlphaFoldDB; P9WMW1; -.
DR SMR; P9WMW1; -.
DR STRING; 83332.Rv1328; -.
DR PaxDb; 83332-Rv1328; -.
DR GeneID; 886886; -.
DR KEGG; mtu:Rv1328; -.
DR TubercuList; Rv1328; -.
DR eggNOG; COG0058; Bacteria.
DR InParanoid; P9WMW1; -.
DR OrthoDB; 9760804at2; -.
DR PhylomeDB; P9WMW1; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR CDD; cd04299; GT35_Glycogen_Phosphorylase-like; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 3.
DR InterPro; IPR011834; Agluc_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR024517; Glycogen_phosphorylase_DUF3417.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR NCBIfam; TIGR02094; more_P_ylases; 1.
DR PANTHER; PTHR42655; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR42655:SF1; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF11897; DUF3417; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Carbohydrate metabolism; Glycogen metabolism;
KW Glycosyltransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..863
FT /note="Glycogen phosphorylase"
FT /id="PRO_0000188556"
FT MOD_RES 618
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 863 AA; 95515 MW; E39826B03D5B374F CRC64;
MKALRRFTVR AHLPERLAAL DQLSTNLRWS WDKPTQDLFA AIDPALWEQC GHDPVALLGA
VNPARLDELA LDAEFLGALD ELAADLNDYL SRPLWYQEQQ DAGVAAQALP TGIAYFSLEF
GVAEVLPNYS GGLGILAGDH LKSASDLGVP LIAVGLYYRS GYFRQSLTAD GWQHETYPSL
DPQGLPLRLL TDANGDPVLV EVALGDNAVL RARIWVAQVG RVPLLLLDSD IPENEHDLRN
VTDRLYGGDQ EHRIKQEILA GIGGVRAIRA YTAVEKLTPP EVFHMNEGHA GFLGIERIRE
LVTDAGLDFD TALTVVRSST VFTTHTPVPA GIDRFPLEMV QRYVNDQRGD GRSRLLPGLP
ADRIVALGAE DDPAKFNMAH MGLRLAQRAN GVSLLHGRVS RAMFNELWAG FDPDEVPIGS
VTNGVHAPTW AAPQWLQLGR ELAGSDSLRE PVVWQRLHQV DPAHLWWIRS QLRSMLVEDV
RARLRQSWLE RGATDAELGW IATAFDPNVL TVGFARRVPT YKRLTLMLRD PDRLEQLLLD
EQRPIQLIVA GKSHPADDGG KALIQQVVRF ADRPQVRHRI AFLPNYDMSM ARLLYWGCDV
WLNNPLRPLE ACGTSGMKSA LNGGLNLSIR DGWWDEWYDG ENGWEIPSAD GVADENRRDD
LEAGALYDLL AQAVAPKFYE RDERGVPQRW VEMVRHTLQT LGPKVLASRM VRDYVEHYYA
PAAQSFRRTA GAQFDAAREL ADYRRRAEEA WPKIEIADVD STGLPDTPLL GSQLTLTATV
RLAGLRPNDV TVQGVLGRVD AGDVLMDPVT VEMAHTGTGD GGYEIFSTTT PLPLAGPVGY
TVRVLPRHPM LAASNELGLV TLA
//
