ID Q9RSD0_DEIRA Unreviewed; 838 AA.
AC Q9RSD0;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE SubName: Full=Alpha-glucan phosphorylase, putative {ECO:0000313|EMBL:AAF11742.1};
GN OrderedLocusNames=DR_2195 {ECO:0000313|EMBL:AAF11742.1};
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230 {ECO:0000313|EMBL:AAF11742.1, ECO:0000313|Proteomes:UP000002524};
RN [1] {ECO:0000313|EMBL:AAF11742.1, ECO:0000313|Proteomes:UP000002524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC NCIMB 9279 / R1 / VKM B-1422 {ECO:0000313|Proteomes:UP000002524};
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L., Utterback T., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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 -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047}.
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DR EMBL; AE000513; AAF11742.1; -; Genomic_DNA.
DR PIR; D75304; D75304.
DR RefSeq; NP_295917.1; NC_001263.1.
DR RefSeq; WP_010888825.1; NZ_JMLF01000004.1.
DR AlphaFoldDB; Q9RSD0; -.
DR STRING; 243230.DR_2195; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR PaxDb; 243230-DR_2195; -.
DR EnsemblBacteria; AAF11742; AAF11742; DR_2195.
DR GeneID; 69518442; -.
DR KEGG; dra:DR_2195; -.
DR PATRIC; fig|243230.17.peg.2420; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_0; -.
DR InParanoid; Q9RSD0; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd04299; GT35_Glycogen_Phosphorylase-like; 1.
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 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002524}.
FT DOMAIN 13..120
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 608
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 838 AA; 93810 MW; F2B5675BB8169ED0 CRC64;
MNVIGKVTVL PQLPAEIARL SELAYNLYWS WTPRAQALYR DLSPELWERF QHNPVRLLLE
ADQDRLNAAA QDPAYLGRYA QVMADFDAYM GKKDTWAARH APQMKPVAYF SMEYAFHESL
PIYSGGLGVL AGDHCKSASD LGLPFTAVGM LFSQGYFRQL FDKDGWQNEA YDELDLTTLP
IQPAQSAAGE DIRVSVRIAG REVAVKVWTL QVGRVRVLLL DSNVPDNSED DRKLTARLYG
GNQELRVQQY VLLGVAGIRA LRALDVPASV YHMNEGHAAL MALERMREYV AAGQDFRTAA
ELAASSTLFT THTPVAAGND AFTYELMDKY IGEWPGLLHA GRDELYALAR HDQQWDGHTV
PAFSMTVFAL SMSRAANGVS ELHGEVSRGM WNFLYPGAEE NEVPIGHVTN GAHNLTFTSQ
RMRDLLSTVL PEDWTERLED ETMWQAVEQL TEEQLSNVQR EMKREMITFV RGRVREQLLR
NGASAADVAA TDNLLDEGTL TIGFARRFAT YKRATLLLRD KPRLAAIVNN PERPVQFVFA
GKAHPADNPG KAFIQEIYRT SQEPEFRGKI VILENYDMNV ARHLVQGVDI WLNNPRRPLE
ASGTSGMKAS FNGSPNFSVL DGWWREGYDG TNGWPIGEER EYADLNVQDD ADAFDLYQRL
EHEIAPRYYG HAQGNASWAH TVRDAIETVS PRFSMQRQVL DYVQQYYLPL GQRGTQLADH
GGARARDLAA WKAWVRQQWP HTSISAQANL PATARPGEQV TVSAQVNPAG IRPEELRVEA
VLKRGDEVQR YPLAPGEGGQ YSAEIPLDDS GLYSVGVRML PLIDGLSNDL EAGLIKWA
//
