ID   A0A2X4TT90_9NOCA        Unreviewed;       839 AA.
AC   A0A2X4TT90;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE            EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN   ORFNames=NCTC10994_01144 {ECO:0000313|EMBL:SQI29609.1};
OS   Rhodococcus coprophilus.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=38310 {ECO:0000313|EMBL:SQI29609.1, ECO:0000313|Proteomes:UP000249091};
RN   [1] {ECO:0000313|EMBL:SQI29609.1, ECO:0000313|Proteomes:UP000249091}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10994 {ECO:0000313|EMBL:SQI29609.1,
RC   ECO:0000313|Proteomes:UP000249091};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) 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; LS483468; SQI29609.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2X4TT90; -.
DR   STRING; 1219011.GCA_001895045_00862; -.
DR   KEGG; rcr:NCTC10994_01144; -.
DR   Proteomes; UP000249091; Chromosome 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000249091};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          3..104
FT                   /note="DUF3417"
FT                   /evidence="ECO:0000259|Pfam:PF11897"
FT   MOD_RES         596
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   839 AA;  92552 MW;  8F6525D0A5FE3C54 CRC64;
     MGTLTANLRW SWHPETQDLF AAVDPELWER CGSDPVRLLG EVPPERLDAL AENEEFLVRL
     DAAAADLDHY LSRPRWYQQQ QERGTAVPAG IAYFSMEFGV SEVLPNYSGG LGILAGDHLK
     AASDLGLPLI GVGLLYRSGY FRQSLSADGW QVEHYPAYDP QGLPIKLLTE ADGSTALVQV
     EIPGGRTLDA RVWIAQIGRV PLLLLDSDIA SNDEELRGVT DRLYGGDQDH RIKQEILAGI
     GGVRAVRAYT RIAGLPDPDV FHMNEGHAGF LGAERIRELV TGTGLDFDEA LAAVRAGTVF
     TTHTPVPAGI DRFPIDLVRH YFSGRNGENE SALLPGLTVD RILALGRESD PDVFNMAHLG
     LRLGQRCNGV SKLHGAVSRN MFEELWPGFD ATEVPIGSVT NGVHAPTWAA REWLALADRL
     AGPDLVEESR GWELLQTVDA RELWEMRNTL RSMLVEEVRR RLRNSWIERG ATEAELGWVD
     SVFEPGVLTI GFARRVPTYK RLTLMLRDPE RLRALLLDPE RPLQLVVAGK SHPADDGGKA
     LIQQVVRFAD EYDVRHRVVF LPDYDMSMAR YLYWGCDVWL NNPLRPLEAC GTSGMKSALN
     GGLNLSIRDG WWDEMYDGEN GWAIPTADGV DDVRRDDLEA NALYELLERS VLPRFYDRDG
     DGVPGRWIEM VRHTLENLGP KVLASRMVRD YAVDYYIPAA AAARSVAADD FAGAKAVAEY
     RERLEAAWPS VRVAQVDTEG LPEVPEIGSR LAVTAHVELG ALAPDDVEVQ AVIGRVGSDD
     SLSDIVSIPM THTGKGSFGE VFEADVRLPL AGPVGYTVRV LPHHDLLASP AEFGMVRLP
//