ID E8UWM6_THEBF Unreviewed; 541 AA.
AC E8UWM6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN OrderedLocusNames=Thebr_0714 {ECO:0000313|EMBL:ADV79308.1};
OS Thermoanaerobacter brockii subsp. finnii (strain ATCC 43586 / DSM 3389 /
OS AKO-1) (Thermoanaerobacter finnii).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=509193 {ECO:0000313|EMBL:ADV79308.1, ECO:0000313|Proteomes:UP000002062};
RN [1] {ECO:0000313|EMBL:ADV79308.1, ECO:0000313|Proteomes:UP000002062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43586 / DSM 3389 / AKO-1
RC {ECO:0000313|Proteomes:UP000002062};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Hemme C.L., Woyke T.;
RT "Complete sequence of Thermoanaerobacter brockii finnii Ako-1.";
RL Submitted (JAN-2011) 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; CP002466; ADV79308.1; -; Genomic_DNA.
DR RefSeq; WP_004400034.1; NC_014964.1.
DR AlphaFoldDB; E8UWM6; -.
DR KEGG; tbo:Thebr_0714; -.
DR HOGENOM; CLU_015112_1_0_9; -.
DR Proteomes; UP000002062; 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; IPR035090; Pyridoxal_P_attach_site.
DR NCBIfam; TIGR02094; more_P_ylases; 2.
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 541 AA; 61581 MW; 9ECBB353FFD13C2B CRC64;
MGNEKLPRVA YFCMEYGLQS DFKLYAGGLG ILAGDHLKAA KELGMPLVGI GILWKQGYTE
QHIGEDGYPY DAYRNYTRKY DFLKDTGVKV KVKIRNRNVY CKVWLIDNFD NAPLYLLDTD
IPENGDRWIT GQLYGWFGEE RVAQEIVLGI GGVRALRALG IDVDVYHFNE GHAVLAAIEL
IREKMENQNM SFEEAWKATR EEVVFTTHTP VKEGNESHDL ELLMYMGANN GLSIEQMAQI
GGVPFNMTVA GLRLSRIANG VSKLHGQTAN KMWQHVDNKA PIISITNGID RNTWVDKRII
EAYNKGEGLL ETHNILKQEL IDFVYQRTGV KLDADKLLIG FSRRAAPYKR SDLIFTNDEV
IGDYLRSKKI QMVFSGKGHP LDDVGKKIVA KLIEMTKKYP ESVVFLEDYD MTIGKMLTRG
TDVWLNNPRR PLEASGTSGM KAAMNGVLNL SILDGWWAEA CIDGVNGWQF GDGFESDNIE
ELDKHDLEAL YDVLLNKVVP TYYNDKAKWE NMMRESIRTT YEAFSANRML KEYYDLMYTK
K
//
