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Database: UniProt
Entry: K7QV13_THEOS
LinkDB: K7QV13_THEOS
Original site: K7QV13_THEOS 
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
//
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