ID   A0A1D8G6Q5_9ACTN        Unreviewed;       895 AA.
AC   A0A1D8G6Q5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE            EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN   Name=malP {ECO:0000313|EMBL:AOT61142.1};
GN   ORFNames=A4G23_04020 {ECO:0000313|EMBL:AOT61142.1};
OS   Streptomyces rubrolavendulae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=285473 {ECO:0000313|EMBL:AOT61142.1, ECO:0000313|Proteomes:UP000095349};
RN   [1] {ECO:0000313|EMBL:AOT61142.1, ECO:0000313|Proteomes:UP000095349}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJM4426 {ECO:0000313|EMBL:AOT61142.1,
RC   ECO:0000313|Proteomes:UP000095349};
RA   Kim J.-G.;
RT   "Streptomyces rubrolavendulae MJM4426 Genome sequencing and assembly.";
RL   Submitted (SEP-2016) 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.
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; CP017316; AOT61142.1; -; Genomic_DNA.
DR   RefSeq; WP_069978057.1; NZ_CP017316.1.
DR   AlphaFoldDB; A0A1D8G6Q5; -.
DR   STRING; 285473.A4G23_04020; -.
DR   KEGG; srn:A4G23_04020; -.
DR   PATRIC; fig|285473.5.peg.4217; -.
DR   OrthoDB; 9760804at2; -.
DR   Proteomes; UP000095349; 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   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   ECO:0000313|EMBL:AOT61142.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000460-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095349};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AOT61142.1}.
FT   DOMAIN          13..141
FT                   /note="DUF3417"
FT                   /evidence="ECO:0000259|Pfam:PF11897"
FT   REGION          101..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         636
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   895 AA;  97919 MW;  5DF51D59054AA22C CRC64;
     MKAIRRFTVR PVLPDPLRPL CDLARNLRWS WHAETRELFQ AVDPEGWRAS GGDPVRLLGT
     VSAARLGELA RDRRFLRRLT AAADDLDDYL HGRRWYQSRT AGDRAAGDRT AGDRTAGGEA
     ADEPPAAIAY FSPEFGVTAA LPQYSGGLGI LAGDHLKAAS DLGVPLIGVG LLYRHGYFRQ
     SLSRDGWQQE HYPLLDPNEL PLTLLRRPDG APVRVGLALP GGGSLHAHVW VAQVGRVPLL
     MLDSDVEENG PGERNVTDRL YGGGSEHRLL QEMLLGMGGV RAVRAYCAVT GHPAPEVFHT
     NEGHAGFLGL ERIRELTDRG TGFDAALEAV RAGTVFTTHT PVPAGIDRFD RELVARHFGP
     GAELPGVDVG RVLQLGRETY PGGDPGVFNM AVMGLRLAQR ANGVSTLHGA VSRSMFAGLW
     PGFDPEEVPI TSITNGVHAP TWVAPEVLRL GARRIGAHRA EDALSVGGSQ RWDAVADLDD
     TAIWELRREL REQLVHEVRA RLRASWRERG AASAELGWID GVLDPDVLTI GFARRVPSYK
     RLTLMLRDRD RLREMLLHPT RPVQIVVAGK AHPADDGGKR LVREMVRFAD DPRVRHRIVF
     LPDYGMAMAK KLYPGCDVWL NNPLRPLEAC GTSGMKAALN GCLNLSVRDG WWDEWYDPDF
     GWAIPTADGP TTDEDRRDDL EAHALYELIE QRVAPRFYDR GANGLPERWI EMVRRTLASL
     GPKVLAGRMV REYVERLYTP AARAHRAMTP DAAGELAEWK ARVRAAWPGV AVDHVEVDEV
     SEIAELGSTL ALRVRVTLGD LTPEDVEVQA VAGRVDTRDG LADARAFPLK PAGGGGPDQQ
     GRWAYEGPLT LDRTGPFGYT VRVLPAHRLL TAGVDLGLVA LPADSAADGA GVLLR
//