ID   C6A428_THESM            Unreviewed;       831 AA.
AC   C6A428;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE            EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN   OrderedLocusNames=TSIB_1321 {ECO:0000313|EMBL:ACS90373.1};
OS   Thermococcus sibiricus (strain DSM 12597 / MM 739).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=604354 {ECO:0000313|EMBL:ACS90373.1, ECO:0000313|Proteomes:UP000009079};
RN   [1] {ECO:0000313|EMBL:ACS90373.1, ECO:0000313|Proteomes:UP000009079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12597 / MM 739 {ECO:0000313|Proteomes:UP000009079};
RX   PubMed=19447963; DOI=10.1128/AEM.00718-09;
RA   Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA   Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT   "Metabolic versatility and indigenous origin of the archaeon Thermococcus
RT   sibiricus, isolated from a siberian oil reservoir, as revealed by genome
RT   analysis.";
RL   Appl. Environ. Microbiol. 75:4580-4588(2009).
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; CP001463; ACS90373.1; -; Genomic_DNA.
DR   RefSeq; WP_015849591.1; NC_012883.1.
DR   AlphaFoldDB; C6A428; -.
DR   STRING; 604354.TSIB_1321; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   GeneID; 8096322; -.
DR   KEGG; tsi:TSIB_1321; -.
DR   eggNOG; arCOG01421; Archaea.
DR   HOGENOM; CLU_015112_0_0_2; -.
DR   OrthoDB; 17863at2157; -.
DR   Proteomes; UP000009079; 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; NF041129; maldex_phorlase_Thcocales; 1.
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:ACS90373.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000460-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009079};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACS90373.1}.
FT   DOMAIN          12..119
FT                   /note="DUF3417"
FT                   /evidence="ECO:0000259|Pfam:PF11897"
FT   MOD_RES         592
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   831 AA;  96739 MW;  6018F048E1B83D5D CRC64;
     MEAVINQIKS KLPENLEGLL DLGYNYWWNW NRRATKLWEK INPEHWREYK NPVKLLLDTP
     EERLKELSKD DDFINLYELV IDQFRHYMES ENTWLSTNWP KWEEPVIYLC MEYGISKSLP
     IYSGGLGILA GDHLKTASDL GLPFIGIGLL YKHGYFKQQI DKNGNQIEVF PEYDPHEMPI
     KPLTTKKGNP ILIEVPIEDR TVYARAFEVN VGRVKLYLLD TDVPENSPDD RTICDYLYNA
     EIDKRIKQEI LLGIGGMRLL RALGIESAVI HLNEGHPAFA NFQRIAWYME EGLNFLEALT
     IVRATTIFTT HTPVPAGHDK FPIVEVEKRL AKFLEGIPKE EFLNLGREGE EFNMTLLSIR
     TSSYVNAVSK LHTAVTKEMW KELWKGVPPD EMPVEGITNG VHTKTWLHNE IKKLIDRYIG
     RVWRDYAELE GLWYGVERIP NEELWEAHLK AKKELIDLIK RNMKERNKRL GIEEPIPEIN
     ENALLIGFAR RFATYKRATM IFNDLERLKK IANNPERPVY IIFGGKAHPM DTSGKEFLKR
     LYEVSQMPEF KGKIIIFENY DMGSARAMIS GVDVWLNTPR RPLEASGTSG MKAGLNGVLN
     LSVYDGWWVE GYNGKNGWII GEESIEPETE GDDITDAESL YELLENEVIP TYYENRQRWI
     YMMKESIKSI APRFSTHRML KEYVNKFYSK ALTNAVLLKR DKFNTTREIA TWKAKVLNSW
     NKVNIERIIT HDAIATEIIV DLDELAPEDV KVEIYYGVKA EGYAIEKPYI IELKRPQHLG
     DTKWLYRYKG NALKNLGNPC WHYAVRVYPY HDKLPHKFLL GLIKWKGFFD F
//