ID   A0A1W2DV07_9PSEU        Unreviewed;       862 AA.
AC   A0A1W2DV07;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE            EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN   ORFNames=SAMN05660733_03310 {ECO:0000313|EMBL:SMD01314.1};
OS   Lentzea albidocapillata.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Lentzea.
OX   NCBI_TaxID=40571 {ECO:0000313|EMBL:SMD01314.1, ECO:0000313|Proteomes:UP000192840};
RN   [1] {ECO:0000313|Proteomes:UP000192840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44073 {ECO:0000313|Proteomes:UP000192840};
RA   Varghese N., Submissions S.;
RL   Submitted (APR-2017) 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; FWYC01000008; SMD01314.1; -; Genomic_DNA.
DR   RefSeq; WP_030481277.1; NZ_JOEA01000027.1.
DR   AlphaFoldDB; A0A1W2DV07; -.
DR   STRING; 40571.SAMN05660733_03310; -.
DR   eggNOG; COG0058; Bacteria.
DR   OrthoDB; 9760804at2; -.
DR   Proteomes; UP000192840; Unassembled WGS sequence.
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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000460-1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          13..133
FT                   /note="DUF3417"
FT                   /evidence="ECO:0000259|Pfam:PF11897"
FT   MOD_RES         619
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   862 AA;  94861 MW;  B66DF984FCC9714A CRC64;
     MRALRRFTVR ASLPEPLSAL STLATNLRWT WHPPTQDLFT SIDPRVWSEV GGDPLRLLSV
     VDAGKLESLA RDDQFLLKLH ALASDLERYV QGPRWYQRRQ DEIVQRREHG APDTPLPTSV
     AYFSMEFGVH EALPNYSGGL GILAGDHLKA ASDLGVPLIA VGLLYRSGYF RQSLSLDGWQ
     IEHYPTLDPR GLPLELLTEP SGLPLLVHVA MPGDRMLRAK IWKAQVGRVP LLLLDSDVEQ
     NDEDLRGVTD RLYGGDQNHR IRQEILAGIG GVRAVRTFCE LTGHAQPEVF HTNEGHAGFL
     GLERIREYIT NEGLDFDQAL TASRAGAVFT THTPVPAGID RFPVDLVQHY FGAENLVPGV
     NTQRILALGA EDNPGMFNMA HMGLRLAQRA NGVSKLHGEV SRDMFRGLWP GFDATEVPIG
     SVTNGVHGPT WAATEMSRLL GASEADSHTS NGLGIGAFEP VTDAGLWELR STLRGRLVDE
     VRRRVRESWL QRGASALELG WTDSVFDPNV LTVGFARRVP TYKRLTLMLR DPERLRSLLL
     HPERPVQLVV AGKSHPADDG GKALIQQIVR YADEAGVRHR IVFLPDYDMS MARYLYWGCD
     VWLNNPMRPL EACGTSGMKA ALNGGLNLSI RDGWWDELYD GSNGWAIPTA DGVNDPVRRD
     DLEANALYDL LGSQVAPLFY DRGEDGVPTR WMSMVRHTLA SLGPVVQASR MVREYVETYY
     APAAASAQNV VGEGYRGAKE LSAYRHRLRA SWTRVRVLDS DLVISGSSVP VLGAPVMVRA
     RVELAGLEPS EVDVQVVLGK VSHDSDELKD IVSAPMSYAG NGNYEAEVPL PHAGALGYTV
     RVLPRHGLLA TSAELGRVVL AG
//