ID Q5JH18_THEKO Unreviewed; 830 AA.
AC Q5JH18;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN OrderedLocusNames=TK1406 {ECO:0000313|EMBL:BAD85595.1};
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014 {ECO:0000313|EMBL:BAD85595.1, ECO:0000313|Proteomes:UP000000536};
RN [1] {ECO:0000313|EMBL:BAD85595.1, ECO:0000313|Proteomes:UP000000536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1
RC {ECO:0000313|Proteomes:UP000000536};
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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; AP006878; BAD85595.1; -; Genomic_DNA.
DR RefSeq; WP_011250357.1; NC_006624.1.
DR AlphaFoldDB; Q5JH18; -.
DR SMR; Q5JH18; -.
DR STRING; 69014.TK1406; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR EnsemblBacteria; BAD85595; BAD85595; TK1406.
DR GeneID; 78447926; -.
DR KEGG; tko:TK1406; -.
DR PATRIC; fig|69014.16.peg.1368; -.
DR eggNOG; arCOG01421; Archaea.
DR HOGENOM; CLU_015112_0_0_2; -.
DR InParanoid; Q5JH18; -.
DR OrthoDB; 17863at2157; -.
DR PhylomeDB; Q5JH18; -.
DR Proteomes; UP000000536; 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 Reference proteome {ECO:0000313|Proteomes:UP000000536};
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 830 AA; 96725 MW; DD3BA3447C39B89A CRC64;
MVNVSNAVED EIRKKLPYPL GDLADLAYNY WWSWNRRATK LWEYIDPEHW REYKNPVKLL
LDTPEERFKE LVRDDDFMNL YELVMDQFHA YMNPRSTWFS TNYPKWDKPI VYLCMEYGIS
KSLPIYSGGL GILAGDHVKT ASDLGLPFIA IGLLYKHGYF RQEIDKDGRQ VEIFPEYKPE
EMPIKPVLDR EGKPLRIEVP IGEGIVYARA FEVNVGRVKL YLLDTDVPEN SPDDRTICDY
LYNAEMDKRI KQEILLGIGG MRLLKALEIE PGVIHLNEGH PAFANLQRIA WYMEEGLTFT
EALSIVRGTT VFTTHTPVPA GHDRFPIEEV KKRLAKFLEG REELLELGRE GDQLNMTLLA
IRTSSYVNGV SQLHAEVSKR MWKDLWPGVP LNEIPIEGIT NGVHTMTWVH NEMRKLFDRY
IGKVWREHTN LEGIWYAVER IPDEELWEAH LQAKREFIDL LRRKAIERNK RLGVDDPIPN
IDENALIIGF ARRFATYKRA TLLLTDLERL KKIVNNPERP VYIVFGGKAH PRDDGGKEFL
RRVYEVSKMP EFRGKIFVME NYDMGSARLM VAGVDVWLNN PRRPMEASGT SGMKAGLNGV
LNVSIYDGWW VEGYNGKNGW VIGEETTEPE TEADDPKDAE SLYTLLEEEV IPTYYENRAK
WIYMMKESIK SIAPRFSTHR MVKEYMDRFY SKAMSNYIWL TRENYSGAKE IAAWKDRVRA
SWDKVEIRDA KAEGNRLEVR VYLDGLKPED VEVELYYGVR AQGYEIEKPH IVELRHPEQV
GEGEWLYTYE GNALRHLGDP CWHYAVRVHP HHEKLPHRFL LGLVKWKGLD
//
