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
//