ID K7QV13_THEOS Unreviewed; 815 AA.
AC K7QV13;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN ORFNames=Theos_1189 {ECO:0000313|EMBL:AFV76231.1};
OS Thermus oshimai JL-2.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=751945 {ECO:0000313|EMBL:AFV76231.1, ECO:0000313|Proteomes:UP000000211};
RN [1] {ECO:0000313|EMBL:AFV76231.1, ECO:0000313|Proteomes:UP000000211}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JL-2 {ECO:0000313|EMBL:AFV76231.1,
RC ECO:0000313|Proteomes:UP000000211};
RX PubMed=23405355; DOI=10.1128/genomeA.00106-12;
RA Murugapiran S.K., Huntemann M., Wei C.L., Han J., Detter J.C., Han C.S.,
RA Erkkila T.H., Teshima H., Chen A., Kyrpides N., Mavrommatis K.,
RA Markowitz V., Szeto E., Ivanova N., Pagani I., Lam J., McDonald A.I.,
RA Dodsworth J.A., Pati A., Goodwin L., Peters L., Pitluck S., Woyke T.,
RA Hedlund B.P.;
RT "Whole Genome Sequencing of Thermus oshimai JL-2 and Thermus thermophilus
RT JL-18, Incomplete Denitrifiers from the United States Great Basin.";
RL Genome Announc. 1:E00106-E00112(2013).
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}.
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DR EMBL; CP003249; AFV76231.1; -; Genomic_DNA.
DR AlphaFoldDB; K7QV13; -.
DR STRING; 751945.Theos_1189; -.
DR KEGG; tos:Theos_1189; -.
DR PATRIC; fig|751945.3.peg.1179; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_0; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000000211; 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; 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 592
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 815 AA; 91407 MW; 2529BF593C07D993 CRC64;
MKVLGRITAM PELPEPLKGL KELAYNLWWS WNPEAAELFQ EIDPVLWKRF RGNPVKLLLE
VDPHRLEALL ATSFPARLQA ILEALRAYLK GKPKVEGPLT AYFSAEFGFH SSLPIYSGGL
GVLAGDHIKA ASDLGLPLLG VGIFYHEGYF HQRLSPEGEQ LEVYEPLHPE ELPLLPVGDR
EGRPLRVGVE FPGRTVWVGA YRVQVGAVPV YLLTTNLPEN APEDRAITAR LYAPGLEMRI
QQEMILGFGG VRVLRALGLF PEAFHMNEGH SAFLGLERLR ELVAQGVAFP EALERVRAGG
IFTIHTPVPA GHDAFPLDLV DRYLGFLYPL LGREEVLALA REEKPWGTVF SMSNLALATA
HQAGGVSALH GEVSRKMFHH LWPDLLLEEV PIGHVTNGVH TWTFLHPRLR RHYGEVFGPE
WLKAPEDPGT WRVEGLGEAF WRIHQELKGD LIREVRRRLY EQRRRNGESP SRLRAAERAL
DPEVLTIGFA RRFATYKRAL LLFKDPERLL KLLQGPYPFQ VVFAGKAHPK DEPGKAYLRE
LVAKIRELGL EDRFVVLEDY DMYLARVLVH GSDVWLNTPR RPLEASGTSG MKAALNGALN
LSVLDGWWAE AYNGKNGFAI GDEREYASEE AQDMADAQSL YDVLESEVLP LFYAKGPEGY
SSGWLSMVHE SLRTVGPRFS AQRMVGEYWG LYQKAKALGE KAQDEALLKA FREALPAFFA
LALRVEAPGD LTLNGTPLEV RARVEGEVPG VLRPFLEVQL LLRRSTGELE ILPLGEEGGV
YRGLFRPPRP GSYTYGLRLA LRHPVTGRVG WVRWA
//