ID   A0A160VUJ8_9EURY        Unreviewed;       836 AA.
AC   A0A160VUJ8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE            EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN   ORFNames=A3L04_05035 {ECO:0000313|EMBL:ASJ16482.1}, CHITON_1740
GN   {ECO:0000313|EMBL:CUX78519.1};
OS   Thermococcus chitonophagus.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=54262 {ECO:0000313|EMBL:CUX78519.1, ECO:0000313|Proteomes:UP000093069};
RN   [1] {ECO:0000313|Proteomes:UP000093069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Vorgias C.E.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CUX78519.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=1 {ECO:0000313|EMBL:CUX78519.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ASJ16482.1, ECO:0000313|Proteomes:UP000250189}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GC74 {ECO:0000313|EMBL:ASJ16482.1,
RC   ECO:0000313|Proteomes:UP000250189};
RA   Oger P.M.;
RT   "Complete genome sequence of Thermococcus chitonophagus type strain GC74.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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; CP015193; ASJ16482.1; -; Genomic_DNA.
DR   EMBL; LN999010; CUX78519.1; -; Genomic_DNA.
DR   RefSeq; WP_068578620.1; NZ_LN999010.1.
DR   AlphaFoldDB; A0A160VUJ8; -.
DR   STRING; 54262.CHITON_1740; -.
DR   GeneID; 33321917; -.
DR   KEGG; tch:CHITON_1740; -.
DR   OrthoDB; 17863at2157; -.
DR   Proteomes; UP000093069; Chromosome i.
DR   Proteomes; UP000250189; 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:CUX78519.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000460-1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CUX78519.1}.
FT   DOMAIN          15..122
FT                   /note="DUF3417"
FT                   /evidence="ECO:0000259|Pfam:PF11897"
FT   MOD_RES         598
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   836 AA;  97200 MW;  B6055045458F0504 CRC64;
     MKIDNSIKEK ILKKLPENLS RLADLAYNYW WSWDHKAMKL WQKIDEEHWR QYKNPVKLLL
     EVPESRLREL SKDDAFLDLY ELVIERFEGY MNQSTTWFST NYPRWDKPIV YLCMEYGISK
     SLPIYSGGLG ILAGDHLKTA SDLGLPLIAV GLLYKHGYFR QEIDKDGRQI EIFPEYNTKE
     MPIRQVLTND GKPLLIDVPI EGKMVKARVF LVEVGRVPLY LLDTDVLENP EEDRKVCDYL
     YNAEPDKRIK QEILLGIGGM RLLKALEIEP GVIHLNEGHP SFANFERIRW FMEEGLSFEE
     ALEVVRGTSV FTTHTPVPAG HDVFPVDFVR EKLAKFFEGL PTEKFLELGK ANPSDPNFNM
     TILSIKTSNF VNGVSQLHAK VTREMWAGLW AGVPLDEIPI EGITNGVHTA TWVNENLAKL
     YDIYIGKIWR EHVNLEGIWY AIERIPDGEL WEAHLKAKRE LIELIRRKIM RRNERIGIDE
     PLPDIDENAL IIGFARRFAT YKRAVLLFTD LERLKKIVNN SERPVYIVFG GKAHPRDEAG
     KEFLRRVYEV SQMPEFKGKI ILIENYDMGS ARLFVSGVDV WLNTPRRPLE ASGTSGMKAG
     LNGVINLSIF DGWWVEGYNG RNGWVIGDTS TEPETEADDY WDAMSLYDIL ENVVVPMYYE
     NRDAWIRMMK ESIKSIAPRF STHRMVKDYV TKFYSKAMEL GIYLSRDNFR WAKELAKWKE
     KIKTEWDKVN IEEVKVNEHI VNVTINLGNL KPEDVRVELY YGIKEEEFKI LKPHIVELRK
     TKDLGNGRYI YTYMGKALKN IGNPCWHYAI RVYAYHPMMP GKFLLGGYIK WKGVER
//