ID D3PQN3_MEIRD Unreviewed; 838 AA.
AC D3PQN3;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN OrderedLocusNames=Mrub_1001 {ECO:0000313|EMBL:ADD27766.1};
GN ORFNames=K649_04645 {ECO:0000313|EMBL:AGK04231.1};
OS Meiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21) (Thermus
OS ruber).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus.
OX NCBI_TaxID=504728 {ECO:0000313|EMBL:AGK04231.1, ECO:0000313|Proteomes:UP000013026};
RN [1] {ECO:0000313|EMBL:ADD27766.1, ECO:0000313|Proteomes:UP000006655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC {ECO:0000313|Proteomes:UP000006655}, and DSM 1279
RC {ECO:0000313|EMBL:ADD27766.1};
RX PubMed=21304689; DOI=10.4056/sigs.1032748;
RA Tindall B.J., Sikorski J., Lucas S., Goltsman E., Copeland A.,
RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A.,
RA Fahnrich R., Goodwin L., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Rohde M., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Meiothermus ruber type strain (21).";
RL Stand. Genomic Sci. 3:26-36(2010).
RN [2] {ECO:0000313|EMBL:AGK04231.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 1279 {ECO:0000313|EMBL:AGK04231.1};
RA Klammer A., Drake J., Heiner C., Clum A., Copeland A., Huddleston J.,
RA Eichler E., Turner S.W.;
RT "Non-Hybrid, Finished Microbial Genome Assemblies from Long-Read SMRT
RT Sequencing Data.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AGK04231.1, ECO:0000313|Proteomes:UP000013026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC {ECO:0000313|Proteomes:UP000013026}, and DSM 1279
RC {ECO:0000313|EMBL:AGK04231.1};
RA Chin J., Alexander D.H., Marks P., Korlach J., Clum A., Copeland A.;
RL Submitted (APR-2013) 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; CP001743; ADD27766.1; -; Genomic_DNA.
DR EMBL; CP005385; AGK04231.1; -; Genomic_DNA.
DR AlphaFoldDB; D3PQN3; -.
DR STRING; 504728.K649_04645; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; mrb:Mrub_1001; -.
DR KEGG; mre:K649_04645; -.
DR PATRIC; fig|504728.9.peg.959; -.
DR eggNOG; COG0058; Bacteria.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000006655; Chromosome.
DR Proteomes; UP000013026; 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 ECO:0000313|EMBL:ADD27766.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADD27766.1}.
FT DOMAIN 13..113
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 594
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 838 AA; 93945 MW; 511F1935DB935F68 CRC64;
MNVIGRIVSM PSLPEALKGL GELAYNLWWS WSPEAQHLFE QINPSQWKRF RANPVRALLE
AEPERLTALA ENAGYVGAVE ATLARFHRYL QSRPQKPPRI AYFSMEYGFH ESLPIYSGGL
GILAGDHIKA ASDLGLDLTA VGMFYHEGYF RQQLTPEGQQ HEIYEDLRPE ELPLVVVSKD
GKPLKVGVEF PGRTVYVMAY KAQVGTIPVY LMSTNLPENR PEDRALTARL YAPGQEIRIE
QEMILGIGGV RLLRALGLAP EVWHMNEGHA AFLGLERMRE MVAAGSSFGE ALEATSAGAL
FTTHTPVPAG HDSFPLDLVE RYLDGWWNKL GISKEEFIAL GREEKSYGPV FSMSNLALHT
SRAAGGVSAL HGEVSREMFK HLWKGLEPEE VPIGHITNGI HTFSFLHPEM HALYERSFPK
TWAEQLHDPS QWTVERLEES ELWHIRNKLR AHLVEEVRAR LFEQRRRNGD LPASLRAAEK
VLDPTVLTIG FARRFATYKR AILMFTDPDR LVSILNGPLP VQFVFAGKAH PKDEPGKEFI
KKLAEKIKGL GLEDKMILLE DYDIGLARTL VQGVDVWLNT PRRPMEASGT SGMKAALNGA
LNFSVLDGWW AEAFNTTNGW AIGDGRTYAT EEAQDYADAQ SFYDTLQYKI IPLFYARGAV
GTPSGWLAMV RDSIRTCGPT YSAQRMVDEY HRKFYTPLAQ RSAHLLEKNA AALKEVADWK
KQVQSAWDNV KVWVEAPSTT INQPLQLRAF VQAYGVPTKT LRVELVVRRN SGDLEVVALQ
HAGQENDALL YTGSYHPARP GSYEYGVRVV ATHPELSSPR EVTFVKWAGA VVEEPVKV
//
