ID D3DFF2_HYDTT Unreviewed; 558 AA.
AC D3DFF2;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN Name=glgP1 {ECO:0000313|EMBL:BAI68554.1};
GN OrderedLocusNames=HTH_0087 {ECO:0000313|EMBL:BAI68554.1};
OS Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6).
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae;
OC Hydrogenobacter.
OX NCBI_TaxID=608538 {ECO:0000313|EMBL:BAI68554.1, ECO:0000313|Proteomes:UP000002574};
RN [1] {ECO:0000313|EMBL:BAI68554.1, ECO:0000313|Proteomes:UP000002574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6534 / IAM 12695 / TK-6 [Tokyo]
RC {ECO:0000313|Proteomes:UP000002574};
RX PubMed=20348262; DOI=10.1128/JB.00158-10;
RA Arai H., Kanbe H., Ishii M., Igarashi Y.;
RT "Complete genome sequence of the thermophilic, obligately
RT chemolithoautotrophic hydrogen-oxidizing bacterium Hydrogenobacter
RT thermophilus TK-6.";
RL J. Bacteriol. 192:2651-2652(2010).
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; AP011112; BAI68554.1; -; Genomic_DNA.
DR RefSeq; WP_012962737.1; NC_017161.1.
DR AlphaFoldDB; D3DFF2; -.
DR STRING; 608538.HTH_0087; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; hth:HTH_0087; -.
DR PATRIC; fig|608538.5.peg.89; -.
DR eggNOG; COG0058; Bacteria.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000002574; 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; 1.
DR PANTHER; PTHR42655; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR42655:SF1; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF00343; Phosphorylase; 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 Reference proteome {ECO:0000313|Proteomes:UP000002574};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 558 AA; 64070 MW; 6150BAE33643F6B7 CRC64;
MIAYFVMELG LEDRIPTYSG GLGTLAGDTL YSFADLSIPA VCITLLYKKG YTLQKITHHG
MQLDFDTLWD YKKVLTPLDV EVRMHFGDKE QKVRAWEYTL RGHGDIKVIF LDTDIPGNEP
DIRRLNERLY LDEGLYRLRQ EMLLGIGGYR VLKALGYNIS VYHKNESHSA LLVVELLREL
GDFQKVRSRC VFTTHTPVPA GHDKFPIDMV KQELKLYDHI DWNKEAIDGF LNLSAFALRY
SCKVNAVSYK HMFVTKNILI DQVPTEGPCE LEYVTNGVYH RRWIHPELQE LFNEYMPAWD
ENPVLLNQVY RVPSELLLKK HNKVKNELVN YINKTTGAGF SDDVLTIGVA RRVTAYKRNN
LILRDIDRLI YVAEHFGELQ IVFAGKAHPK DSMGKEMIAD IFSKIQALKQ RTSKVKVAFL
ENYSIDMAKL LVAGCDVWLN NPKRPYEACG TSGMKAAMNG VLNFSTWDGW WLEGGIEGIN
GWGIGPRPSW SDMSESNDEE DLEDIYGKLA YVILPMYYTS KDQWVFMMKN SIATVGPFFN
THRMVSEYIS KVYQIGLR
//
