ID F7YW48_9THEM Unreviewed; 566 AA.
AC F7YW48;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN ORFNames=Theth_0442 {ECO:0000313|EMBL:AEH50537.1};
OS Pseudothermotoga thermarum DSM 5069.
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Pseudothermotoga.
OX NCBI_TaxID=688269 {ECO:0000313|EMBL:AEH50537.1, ECO:0000313|Proteomes:UP000006804};
RN [1] {ECO:0000313|EMBL:AEH50537.1, ECO:0000313|Proteomes:UP000006804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5069 {ECO:0000313|EMBL:AEH50537.1,
RC ECO:0000313|Proteomes:UP000006804};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Ivanova N., Zeytun A., Brettin T., Detter J.C.,
RA Tapia R., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Thermotoga thermarum DSM 5069.";
RL Submitted (NOV-2010) 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}.
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DR EMBL; CP002351; AEH50537.1; -; Genomic_DNA.
DR AlphaFoldDB; F7YW48; -.
DR STRING; 688269.Theth_0442; -.
DR KEGG; tta:Theth_0442; -.
DR PATRIC; fig|688269.3.peg.452; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_1_0_0; -.
DR Proteomes; UP000006804; 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; 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; PF00343; Phosphorylase; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000006804};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 566 AA; 64727 MW; 9489C8F8D909609F CRC64;
MKINPKRRKI AYFSMEIGLN EKMHTYSGGL GILAGDTLKS AADLEIPMVA VTLLNRYGYF
KQELTHDGQQ IEHPDPWPVE EFLTKEDVKV SVRIEGRSVR VTAWRYDVVG VTGYVVPVYF
LDTYLEENSE YDRKLTDYLY GGDQKYRLCQ EVVLGIGGVR ILRALGYDEI ETFHMNEGHS
ALLTFELIDE ELRKTSSSMI LESHLKAVRE KCVFTTHTPV PAGHDKFPLE LVRKVIGPRD
ELFSLPQVVY DNTLNMTYLA LNMSRYINGV AKKHGEVSKL MFAGYDISSI TNGVHAQTWV
SEPFQELFDK YIPMWRTDNF SLRYALSIPN EEIWNAHMKC KKTLLEYVKT QTGVEMNEEV
LTIGFARRAT AYKRADLLLY NLERLKEISS KDGKIQVIYA GKAHPKDEGG KQLIKKIFTA
IQELKSHVPM VYLPNYDMKV AKMMVSGVDI WLNTPQPPLE ASGTSGMKAS LNGVPNFSVL
DGWWIEGCIE GITGWAIGDF SENASSEQHA KSLYEKLEKT IIPLYYQHRD QFIQMMKYAI
AINGSFFNTH RMVQEYVINA YFHKES
//
