ID F4HI89_PYRSN Unreviewed; 836 AA.
AC F4HI89;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN OrderedLocusNames=PNA2_0098 {ECO:0000313|EMBL:AEC51016.1};
OS Pyrococcus sp. (strain NA2).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=342949 {ECO:0000313|EMBL:AEC51016.1, ECO:0000313|Proteomes:UP000008293};
RN [1] {ECO:0000313|EMBL:AEC51016.1, ECO:0000313|Proteomes:UP000008293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA2 {ECO:0000313|EMBL:AEC51016.1,
RC ECO:0000313|Proteomes:UP000008293};
RX PubMed=21602357; DOI=10.1128/JB.05150-11;
RA Lee H.S., Bae S.S., Kim M.S., Kwon K.K., Kang S.G., Lee J.H.;
RT "Complete genome sequence of hyperthermophilic Pyrococcus sp. strain NA2,
RT isolated from a deep-sea hydrothermal vent area.";
RL J. Bacteriol. 193:3666-3667(2011).
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; CP002670; AEC51016.1; -; Genomic_DNA.
DR RefSeq; WP_013747574.1; NC_015474.1.
DR AlphaFoldDB; F4HI89; -.
DR STRING; 342949.PNA2_0098; -.
DR GeneID; 10553554; -.
DR KEGG; pyn:PNA2_0098; -.
DR PATRIC; fig|342949.8.peg.98; -.
DR eggNOG; arCOG01421; Archaea.
DR HOGENOM; CLU_015112_0_0_2; -.
DR OrthoDB; 17863at2157; -.
DR Proteomes; UP000008293; 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; 2.
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 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; 97195 MW; 741B918E71CCB8E6 CRC64;
MKVDNSIKEK ILSKLPENLT KLADLAYNYW WSWDPKAMKL WQKIDEEHWR EYKNPVKLLL
ETPESRLRSL ARDDSFLDLY ELVIERFEDY MKESSTWFST NYPGWDKPII YLCMEYGIGK
SLPIYSGGLG ILAGDHLKTA SDLGLPLIAI GLLYKHGYFK QEIDREGRQI EKFPEYNIRE
MPLRQVLDND GSPLLVDVPI EDRIVKARVF LVDVGRVKLY LLDTDVPENS EEDRKICDYL
YNAEPEKRIK QEILLGIGGM RLLKKLEIEP GVIHLNEGHP AFANFERIRW FLERGLSFSE
ALEVVRGTSV FTTHTPVPAG HDVFPIDFVR EKLRAFLNGL PEEEFLSLGR VNETDPNFNM
TVLAIRTSNF VNAVSKLHAK VTREMWKNLW PGVPQDEIPI EAITNGVHTP TWVNENLAKL
YDIYLGKMWR EHVNLEGIWY AIERIPDDEL WEAHLKAKRE LIELIRRKIM KRNERLGIDE
PLPDIDENAL IIGFARRFAT YKRAILLFTD LERLKRIINN PERPVYIIFG GKAHPMDAEG
KEYLRRVYEV SQMPEFKGKI ILIENYDLGS ARILISGVDV WLNTPRRPLE ASGTSGMKAG
LNGVVNLSTF DGWWVEGYNG RNGWVIGDAT LEPESEEDDY LDAMSLYDLL ENVVIPTYYE
NREAWIRLMK ESIKSIAPRF STYRMLKEYM TKFYSRAMEM GIYLSRDGFK WAKELAKWKE
KIRKEWSNVE IEEVKVENGT VNVTIRLGNL SPDDVRVELY YGVKGDGKIA EPYTVELRSV
AKLEDGRYLY IYSGKALKYL NNGCWHYSIR VYAYHPMIPG KFLLGGYIKW KDIKEG
//
