ID B9DRS9_STRU0 Unreviewed; 801 AA.
AC B9DRS9;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=glgP {ECO:0000313|EMBL:CAR41538.1};
GN OrderedLocusNames=SUB0665 {ECO:0000313|EMBL:CAR41538.1};
OS Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=218495 {ECO:0000313|EMBL:CAR41538.1, ECO:0000313|Proteomes:UP000000449};
RN [1] {ECO:0000313|Proteomes:UP000000449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-854 / 0140J {ECO:0000313|Proteomes:UP000000449};
RX PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA Parkhill J.;
RT "Evidence for niche adaptation in the genome of the bovine pathogen
RT Streptococcus uberis.";
RL BMC Genomics 10:54-54(2009).
CC -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC glucose-1-phosphate, and plays a central role in maintaining cellular
CC and organismal glucose homeostasis. {ECO:0000256|RuleBase:RU000587}.
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|RuleBase:RU000587};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000587};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR EMBL; AM946015; CAR41538.1; -; Genomic_DNA.
DR RefSeq; WP_012658183.1; NC_012004.1.
DR AlphaFoldDB; B9DRS9; -.
DR STRING; 218495.SUB0665; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; sub:SUB0665; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_9; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000000449; 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 CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR NCBIfam; TIGR02093; P_ylase; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF3; GLYCOGEN PHOSPHORYLASE; 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 Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU000587,
KW ECO:0000313|EMBL:CAR41538.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1,
KW ECO:0000256|RuleBase:RU000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000000449};
KW Transferase {ECO:0000256|RuleBase:RU000587, ECO:0000313|EMBL:CAR41538.1}.
FT MOD_RES 648
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 801 AA; 92057 MW; 19597B2D161E1E39 CRC64;
MKVTKEKFIR DFKDTLHEEQ LVKIPNASET EIFLALAKLV RKYYTRIWLE RNRQLTENQE
KVAYYFSIEF LPGRMLETNL LNLGILSTTK EAFNELEIDF EAVKEAEHDM ALGNGGLGRL
AAAFMDSLAT TGYPGFGNGL RYQYGLFKQR IVDGYQVELP DTWFGSTGNV WEVRKDHDIV
DVKLFGNVYL KSNDDGKLVP VYEGAQVLKA VPYDVPQIGF GNDVINNLRL WDVEIPLENE
LDYPTLESRR AVQDITAVLY PDDSNYEGKK LRLIQEYFMT SAGLQTIIKS YLKQGMPLKD
IYQKVSVHIN DTHPAVAPAE LMRLLIDDYG MEWDEAWEAT IKTMSYTNHT ILSEALEKWD
TELFKFVLPR VYQIILEIDN RYVKDLAQKG IEAELIEHTR IVKDRFIHMA HLAIIGGHSV
NGVAKLHTEL LKEDTLRAFY QLYPEKFNNK TNGIVQRRWT QIAAPELSRV IDSTIGVDWR
RDIHLLRELE NFQNDPQVLK QFHQVKQIAK EKLAKYILKT TGVVVSTDAI FDVQVKRLHA
YKRQLLNVLH IMKRYLDLKD NPDLDCLPRV FIFGAKAAPG YHFAKSVIKI INEMANLINN
DASLNGKLKV VFLENYNVSL AELIIPAADV SEQISLASKE ASGTSNMKFM MTGAITLATL
DGANIEIKDE VGDDNIIIFG MTKDQVYDHY AKHDYNSRMI YENNPEIKCI IDSFVNGTIP
NCQSEGMEIY EALITHNDEY FLLEDLPAYI EAQDKIDLLY RNQMKWTQMS LLNIAHSDKF
TSDDTIEEYA KEIWDLKKSI N
//
