ID   A0A1W6WB14_9FIRM        Unreviewed;       814 AA.
AC   A0A1W6WB14;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   ORFNames=B6259_00300 {ECO:0000313|EMBL:ARP49466.1};
OS   Ruminococcaceae bacterium CPB6.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX   NCBI_TaxID=1572656 {ECO:0000313|EMBL:ARP49466.1, ECO:0000313|Proteomes:UP000195433};
RN   [1] {ECO:0000313|EMBL:ARP49466.1, ECO:0000313|Proteomes:UP000195433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CPB6 {ECO:0000313|EMBL:ARP49466.1,
RC   ECO:0000313|Proteomes:UP000195433};
RA   Tao Y.;
RT   "Complete genome sequence of Ruminococcaceae bacterial strain CPB6.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC       glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC       glucose-1-phosphate, and plays a central role in maintaining cellular
CC       and organismal glucose homeostasis. {ECO:0000256|RuleBase:RU000587}.
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|RuleBase:RU000587};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU000587};
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR   EMBL; CP020705; ARP49466.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6WB14; -.
DR   STRING; 1572656.B6259_00300; -.
DR   KEGG; rbp:B6259_00300; -.
DR   OrthoDB; 9760804at2; -.
DR   Proteomes; UP000195433; 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; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR011833; Glycg_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   NCBIfam; TIGR02093; P_ylase; 1.
DR   PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR   PANTHER; PTHR11468:SF3; GLYCOGEN PHOSPHORYLASE; 1.
DR   Pfam; PF00343; Phosphorylase; 1.
DR   PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU000587};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1,
KW   ECO:0000256|RuleBase:RU000587};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195433};
KW   Transferase {ECO:0000256|RuleBase:RU000587}.
FT   MOD_RES         654
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   814 AA;  92788 MW;  306A7693F56EFEA2 CRC64;
     MEYKHSVPQI EKQILAKLEH GYGVGLENAT NDQIYKSVAL IAREMMEQGC SEFMAEAEKT
     KTKQVYYLCM EFLLGRSLKN TLFNLGVEND FREALRQMGV KLDSLYDCEP DAGLGNGGLG
     RLAACFMDAL ATQRYPAMGY SLCYEYGIFR QKLVDGWQTE LPDFWLPGGR IWMHEIPEKA
     VEVHFRGHVE ERWHNNYHEC IHKDYTTIMA VPCDMYIAGM DGKGVSRLRL WKSKGESFDM
     GLFNSGNYMR AMEQNAMAES ITKVLYPEDN HPEGKSLRLT QQYFLVSASI QDIIRTHLFQ
     YATLDNLPDT VAIHLNDTHP VLAIPELMRI MLDECGYDWD HAWDITTRTV AYTNHTVMKE
     ALECWSQELF KMQLPRIYQI VEEINRRFCQ QMHDIGVDGY KVGRMAPLND GYVKMANLAV
     VGSHSVNGVS ALHSDILKKT VFNDFYTEMP EKFTNVTNGI AHRRWLNQSN PELANLLTQK
     IGRGYIYDAS QLKKLEAFKD DKAVLKELAE IKHHNKERLA AYIKKENNVT VDPDSIFDVQ
     VKRMHEYKRQ HLNALNILAT YLWLKDNPNA DFVPHTYIFG AKAAPGYYFA KQMIRFIYKL
     GQLINNDPAV NQKMKVIYIE DYRVTLAELL IPAADISEQI SLAGTEASGT SNMKFMINGA
     VTLGTLDGAN VEIHDSVGDD NMLLFGMTTP EVEILRKDGY HPEQIYYNNP AVHCAIDYMR
     GGVNGVEFGD IVHSLTTNDP YMVLADFDSY QKAQGRAVKL YRNPETWQRM CLINIANAGR
     FAADRAIREY ADNIWHCKPV PSSTAPGTDA FATK
//