PHSG_CHLPN
ID PHSG_CHLPN Reviewed; 824 AA.
AC Q9Z8N1; Q9JQ49;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Glycogen phosphorylase;
DE EC=2.4.1.1;
GN Name=glgP; OrderedLocusNames=CPn_0307, CP_0451, CpB0316;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000305}.
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DR EMBL; AE001363; AAD18456.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38289.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98517.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98249.1; -; Genomic_DNA.
DR PIR; C72095; C72095.
DR PIR; C86529; C86529.
DR RefSeq; NP_224512.1; NC_000922.1.
DR AlphaFoldDB; Q9Z8N1; -.
DR SMR; Q9Z8N1; -.
DR STRING; 115711.CP_0451; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR EnsemblBacteria; AAD18456; AAD18456; CPn_0307.
DR EnsemblBacteria; AAF38289; AAF38289; CP_0451.
DR KEGG; cpa:CP_0451; -.
DR KEGG; cpj:glgP; -.
DR KEGG; cpn:CPn_0307; -.
DR KEGG; cpt:CpB0316; -.
DR PATRIC; fig|115713.3.peg.341; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_0; -.
DR OrthoDB; 137158at2; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; Chromosome.
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; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR PANTHER; PTHR11468; PTHR11468; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR TIGRFAMs; TIGR02093; P_ylase; 1.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; Carbohydrate metabolism; Glycogen metabolism;
KW Glycosyltransferase; Pyridoxal phosphate; Transferase.
FT CHAIN 1..824
FT /note="Glycogen phosphorylase"
FT /id="PRO_0000188551"
FT MOD_RES 667
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 824 AA; 94517 MW; B71EA8654A3ECBAC CRC64;
MEDFSSFDKN KVSVDSMKRA ILDRLYLSVV QSPESASPRD IFTAVAKTVM EWLAKGWLKT
QNGYYKNDVK RVYYLSMEFL LGRSLKSNLL NLGILDLVRK ALKTLNYDFD HLVEMESDAG
LGNGGLGRLA ACYLDSMATL AVPAYGYGIR YDYGIFDQRI VNGYQEEAPD EWLRYGNPWE
ICRGEYLYPV RFYGRVIHYT DSRGKQVADL VDTQEVLAMA YDIPIPGYGN DTVNSLRLWQ
AQSPRGFEFS YFNHGNYIQA IEDIALIENI SRVLYPNDSI TEGQELRLKQ EYFLVSATIQ
DIIRRYTKTH ICLDNLADKV VVQLNDTHPA LGIAEMMHIL VDREELPWDK AWEMTTVIFN
YTNHTILPEA LERWPLDLFS KLLPRHLEII YEINSRWLEK VGSRYPKNDD KRRSLSIVEE
GYQKRINMAN LAVVGSAKVN GVSSFHSQLI KDTLFKEFYE FFPEKFINVT NGVTPRRWIA
LCNPRLSKLL NETIGDRYII DLSHLSLIRS FAEDSGFRDH WKGVKLKNKQ DLTSRIYNEV
GEIVDPNSLF DCHIKRIHEY KRQLMNILRV IYVYNDLKEN PNQDVVPTTV IFSGKAAPGY
VMAKLIIKLI NSVADVVNQD SRVNDKLKVL FLPNYRVSMA EHIIPGTDLS EQISTAGMEA
SGTGNMKFAL NGALTIGTMD GANIEMAEHI GKENMFIFGL LEEQIVQLRR EYCPQTICDK
NPKIRQVLDL LEQGFFNSND KDLFKPIVHR LLHEGDPFFV LADLESYIAA HENVNKLFKE
PDSWTKISIY NTAGMGFFSS DRAIQDYARD IWHVPTKSCS GEGN
