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PHSG_MYCTU
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   25-MAY-2022, entry version 37.
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; 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   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.m111.011627;
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).
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; P9WMW1; -.
DR   GeneID; 886886; -.
DR   KEGG; mtu:Rv1328; -.
DR   TubercuList; Rv1328; -.
DR   eggNOG; COG0058; Bacteria.
DR   OMA; LYRHGYF; -.
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   InterPro; IPR011834; Agluc_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   InterPro; IPR024517; Glycogen_phosphorylase_DUF3417.
DR   InterPro; IPR035090; Pyridoxal_P_attach_site.
DR   Pfam; PF11897; DUF3417; 1.
DR   Pfam; PF00343; Phosphorylase; 2.
DR   PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR   TIGRFAMs; TIGR02094; more_P_ylases; 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
 
 
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