ID   A0A6G6WEW8_9ACTN        Unreviewed;       859 AA.
AC   A0A6G6WEW8;
DT   12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT   12-AUG-2020, sequence version 1.
DT   18-JUN-2025, entry version 17.
DE   RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE            EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN   ORFNames=G5V58_14260 {ECO:0000313|EMBL:QIG43774.1};
OS   Nocardioides anomalus.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=2712223 {ECO:0000313|EMBL:QIG43774.1, ECO:0000313|Proteomes:UP000502996};
RN   [1] {ECO:0000313|EMBL:QIG43774.1, ECO:0000313|Proteomes:UP000502996}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R-3366 {ECO:0000313|EMBL:QIG43774.1,
RC   ECO:0000313|Proteomes:UP000502996};
RA   Im W.-T.;
RT   "Full genome sequence of Nocardioides sp. R-3366.";
RL   Submitted (FEB-2020) 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; CP049257; QIG43774.1; -; Genomic_DNA.
DR   RefSeq; WP_165233930.1; NZ_CP049257.1.
DR   AlphaFoldDB; A0A6G6WEW8; -.
DR   KEGG; nano:G5V58_14260; -.
DR   Proteomes; UP000502996; Chromosome.
DR   GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 3.
DR   InterPro; IPR011834; Agluc_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   InterPro; IPR052182; Glycogen/Maltodextrin_Phosph.
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   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
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:UP000502996};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:QIG43774.1}.
FT   DOMAIN          13..120
FT                   /note="DUF3417"
FT                   /evidence="ECO:0000259|Pfam:PF11897"
FT   MOD_RES         615
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   859 AA;  94665 MW;  C22E095C0BF1CCB7 CRC64;
     MRAIRRFTVR PVLPEALSAL GDLANNLRWS WHPPTQDVFA EVDPELWEST GRDPVKLLGA
     VPKARFEELA SDPGFVERLG AVQADLTAYL TEDRWYQRKV QDGPRAIGYF SPEFGITAVL
     PQYSGGLGIL AGDHLKAASD LGTPIIGVGL LYKHGYFKQS LSREGWQQES YPVLDPDGMP
     ISLLREADGT RASIEIEMPD GPPLVARIWV ASVGRVPLLM LDTDVEGNPQ HFVDITDRLY
     GGNSEHRLRQ ELLLGVGGVR ALRVFCRLTG HPAPEVFHTN EGHAGFLGIE RIRELTVAED
     GPKVDWDTAL EMGRASTVFT THTPVPAGID RFPRTLVEQY FPGETGATPG VPLEKLLALG
     TEDYAGGDAT VFNMAVMGFR LAQRANGVSQ LHGHVSREMF NGLWPAFDEA EVPIGSITNG
     VHAPSWVARE MFDLAASQGA DVHTDDVEAF LSVVDKVPGN EVWAVKRVLR ERLVKDARRR
     LASSWRKRGA AAAELKWIDN ALDPDVLTIG FARRAASYKR LTLMMRDPER LKRLLLHPER
     PIQLVIAGKA HPADDGGKKL IQDIVRLSDD PELRHRIVFL PNYDIAMAKP LYPGCDVWLN
     NPLRPYEACG TSGMKAALNG GLNLSILDGW WDEWYDGDNG WAIPTADGVD DVDKRDDLEA
     EALYDLIEND VAPRFYDHDH EGVPGRWLEM VRHTLKSLGP KVLATRMVRD YVRDLYAPAC
     HNARLLNADY TGAATLAAWK KRVKSAWLSV RVEHVESSGV GDAAEVGAVL SVRAFVSLGD
     LAPDDVHVQV LHGKIDSNDV LADVTVRDLA LAETYDGGRY RFDGDVELDR GGPFGYTVRV
     IPRNELLTSV AELGVVAVA
//