ID W2U7W2_9DEIN Unreviewed; 818 AA.
AC W2U7W2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN ORFNames=TNMX_01955 {ECO:0000313|EMBL:ETN89407.1};
OS Thermus sp. NMX2.A1.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=570924 {ECO:0000313|EMBL:ETN89407.1, ECO:0000313|Proteomes:UP000018848};
RN [1] {ECO:0000313|EMBL:ETN89407.1, ECO:0000313|Proteomes:UP000018848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NMX2.A1 {ECO:0000313|EMBL:ETN89407.1,
RC ECO:0000313|Proteomes:UP000018848};
RA Litthauer D., van Heerden E., Tlalajoe N.;
RT "The genome sequence of Thermus sp. NMX2.A1.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylase is an important allosteric enzyme in
CC carbohydrate metabolism. Enzymes from different sources differ in their
CC regulatory mechanisms and in their natural substrates. However, all
CC known phosphorylases share catalytic and structural properties.
CC {ECO:0000256|ARBA:ARBA00025174}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETN89407.1}.
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DR EMBL; ATNI01000027; ETN89407.1; -; Genomic_DNA.
DR AlphaFoldDB; W2U7W2; -.
DR PATRIC; fig|570924.3.peg.362; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000018848; Unassembled WGS sequence.
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; 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 13..113
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 818 AA; 92191 MW; 6ABD6BD5D1D877B2 CRC64;
MRVLGRLTAM PELPEALRGL RKLAYNLWWS WNPEAAELFQ EIDSSLWKPF RGNPVKLLLE
VDPARLEALA GSTYPARVQA VVAALEAYLK EREEKQGPPT AYFSAEYGFH SSLPIYAGGL
GVLAGDHIKA ASDLGLNLVG VGIFYHEGYF HQRLSPEGAQ VEVYETLHPE ELPLLPVQDR
GGHPLRVGVE FPGRTVWLGA FQVQVGAVPV YLLTADLPEN APEDRAITAR LYAPGLEMRI
QQEMVLGIGG IRLLRALGLN PQVFHMNEGH SAFLGLERVR ELVAEGYTFP VALELARAGA
LFTTHTPVPA GHDAFPLELV ERYLLGFWEK LSVDKEGFFA LGLEEKPWGK VFSMSNLALR
TSAQAGGVSR LHGEVSREMF HHLWPELLRE EVPIGHITNG VHTWTFLHPR LRRHYAEVFG
PDWLRHPEDP ATWRVEGLGE EFWRIHRDLR AELVREVRSR LYEQRRRNGE SPSRLRQAER
LLDPEALTVG FARRFATYKR AVLLFKDPER LLRILQGPYP VQFVFAGKAH PKDEPGKAYL
QELVARIKEY GLEDRMVVLE DYDMYLARVL VHGSDVWLNT PRRPMEASGT SGMKAALNGV
LNLSVLDGWW AEAYNGKNGF AIGDERVYEN EEAQDMADAQ ALYDVLEGEV LPLFYAKGPE
GYSSGWLSMV HESLRTVGPR FSAARMVREY LALYQRGQEW AGKARGEEEV LRAFHQALPA
FYGLALRVEV PGDLTLNGEP LRARAYLEGE VPEALRPFLE VQLVVRRAGG GLEVVPMEEA
SGWFEVAYRP SRPGSYAYGV RMALRHPVTG RVEWVRWA
//
