ID Q82JF5_STRAW Unreviewed; 878 AA.
AC Q82JF5;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN Name=glgP {ECO:0000313|EMBL:BAC70511.1};
GN ORFNames=SAVERM_2800 {ECO:0000313|EMBL:BAC70511.1};
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=227882 {ECO:0000313|EMBL:BAC70511.1, ECO:0000313|Proteomes:UP000000428};
RN [1] {ECO:0000313|EMBL:BAC70511.1, ECO:0000313|Proteomes:UP000000428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2] {ECO:0000313|EMBL:BAC70511.1, ECO:0000313|Proteomes:UP000000428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
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.
CC {ECO:0000256|ARBA:ARBA00025174}.
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 Evidence={ECO:0000256|ARBA:ARBA00001275};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047}.
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DR EMBL; BA000030; BAC70511.1; -; Genomic_DNA.
DR RefSeq; WP_010984232.1; NZ_JZJK01000071.1.
DR AlphaFoldDB; Q82JF5; -.
DR KEGG; sma:SAVERM_2800; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_11; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000000428; 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:0005975; P:carbohydrate 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 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000428};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..126
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 621
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 878 AA; 97014 MW; BE24C8F3DEBC6EC1 CRC64;
MKAIRRFTVR PVLPDALHPL SDLARNLRWS WHAETRELFQ SVDPERWAAS DGDPVRLLGS
VPHARLAELA EDRRFLRRLG AAADDLTDYV TGDRWYQSQA EAPSRAAELP AAIAYFSPEF
GVTAALPQYS GGLGILAGDH LKAASDLGVP LIGVGLLYRH GYFRQSLSRD GWQQEHYPVL
DPHELPVVPL REDDGALAQV SLALPGGRRL QARIWLAQVG RVPLLMLDSD VEENDHGERG
VTDRLYGGGS EHRLLQEMLL GIGGVRAVRT YCRLTGHAEP EVFHTNEGHA GFLGLERIAE
LCDTGLDFDA GLESVRAGTV FTTHTPVPAG IDRFDRELVA RHFGPDAELP RIDVERILGL
GMETYPGGEP NLFNMAVMGL RLGQRANGVS LLHGQVSREM FSGLWPGFDP DEVPITSVTN
GVHAPTWVAP EVFRLGARQI GAQRTEDAMT VGGSERWDAV AEIPDQDIWD LRRVLREQLV
TEVRERLRAS WRQRGAGTAE LGWIDGVLDP DVLTIGFARR VPSYKRLTLM LRDRDRLMDL
LLHPERPVQI VVAGKAHPAD DGGKRLVQEL VRFADDPRVR HRIVFLPDYG MAMAQKLYPG
CDIWLNNPLR PLEACGTSGM KAALNGCLNL SVLDGWWDEW FQPDFGWAIP TADGTATDED
RRDDLEATAL YDLLEGRVAP RFYERGQAGL PDRWIEMVRQ TLTHLGPKVL AGRMVREYVE
RLYTPAALAH RALTPEPARE LATWKSRVRA AWPRVTVDHV ETSVATTTAE LGTTLSLRVR
VGLGDLDPDD VEVQAVAGRV DGQDRITDAT AVPLKPVGGP DLEGRRVYEG PLSLDRTGPF
GYTVRILPTH RLLATSAELG LVAVPSEDVG EGAGVLLR
//
