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Database: UniProt/TrEMBL
Entry: W8NRA3_9EURY
LinkDB: W8NRA3_9EURY
Original site: W8NRA3_9EURY 
ID   W8NRA3_9EURY            Unreviewed;       832 AA.
AC   W8NRA3;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE            EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN   ORFNames=BD01_0029 {ECO:0000313|EMBL:AHL21662.1};
OS   Thermococcus nautili.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=195522 {ECO:0000313|EMBL:AHL21662.1, ECO:0000313|Proteomes:UP000019434};
RN   [1] {ECO:0000313|EMBL:AHL21662.1, ECO:0000313|Proteomes:UP000019434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=30-1 {ECO:0000313|EMBL:AHL21662.1,
RC   ECO:0000313|Proteomes:UP000019434};
RA   Oberto J., Gaudin M., Cossu M., Gorlas A., Slesarev A., Marguet E.,
RA   Forterre P.;
RT   "Genome Sequence of an Hyperthermophilic Archaeon, Thermococcus nautili 30-
RT   1, producing viral vesicles.";
RL   Submitted (FEB-2014) 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; CP007264; AHL21662.1; -; Genomic_DNA.
DR   RefSeq; WP_042688677.1; NZ_CP007264.1.
DR   AlphaFoldDB; W8NRA3; -.
DR   STRING; 195522.BD01_0029; -.
DR   GeneID; 24958045; -.
DR   KEGG; tnu:BD01_0029; -.
DR   eggNOG; arCOG01421; Archaea.
DR   HOGENOM; CLU_015112_0_0_2; -.
DR   OrthoDB; 17863at2157; -.
DR   Proteomes; UP000019434; 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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000460-1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          16..123
FT                   /note="DUF3417"
FT                   /evidence="ECO:0000259|Pfam:PF11897"
FT   MOD_RES         594
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   832 AA;  97060 MW;  C9D488C902C7E3F9 CRC64;
     MARVDECTYE TIRERLPSPL RGLADLAYNY WWSWNRRATK LWEKIDPEHW AEYKNPVKLL
     LDTPPHRFRE LLRDDDFMNL YELVMEQFED YMNPDSTWFS TNYPNWDKPI VYLCMEYGIS
     KSLPIYSGGL GILAGDHVKT ASDLGLPFIA VGLLYKHGYF RQEIDENGNQ IEVFPEYRPE
     EMPIKPVLDR NGERLLIEVP IEDRTVYARA FEVQVGRVRI YLLDTDVPEN GEDDRKICDY
     LYNAEMDKRI KQEILLGIGG MRLLKALGIE PGVVHLNEGH PAFANLQRIA WLMDEGLTFT
     EALSVVRGTT VFTTHTPVPA GHDRFPIEEV RKRLAKFLEG REELLELGRE GDHLNMTLLA
     IRTSSYVNGV SRLHAEVSRR MWQDLWPGVP LDEIPIEPIT NGVHTMTWVH NEMRKLFDRY
     IGKVWREHTN LEGIWYAVER IPDEELWEAH LEAKRQFIEL LRRKAMERNE RLGTDDPIPA
     IDENALIIGF ARRFATYKRA VLLLTDLDRL RKLLNDPTRP VYIVFGGKAH PNDWGGKEFL
     RRIYEVSKMP EFRGKIFVME NYDMGSARLM VAGVDVWLNT PRRPLEASGT SGMKAGLNGV
     LNASIFDGWW VEGYNGKNGW VIGEESTEPE SEADDVKDAQ ALYDLLEREI IPTYYGNRPK
     WIYMMKESIK SIAPRFSTHR MVKEYMDKFY SKAMSNHIWL TRENYRGARE IAEWKDRVTE
     SWPKVGFVDV KVFDDRSGLE VTVDLDGLKP EDVRVELYYG VRAEGYHIER PHIVELRHPK
     RLEGGKWLYT YRGSALRHLG DPCWHYALRV YPHHEKLPHK FLLGLVKWVG LD
//
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