ID A0A0J1G0H4_9FIRM Unreviewed; 818 AA.
AC A0A0J1G0H4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=RHS_5085 {ECO:0000313|EMBL:KLU69099.1};
OS Robinsoniella sp. RHS.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Robinsoniella.
OX NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU69099.1, ECO:0000313|Proteomes:UP000036477};
RN [1] {ECO:0000313|EMBL:KLU69099.1, ECO:0000313|Proteomes:UP000036477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHS {ECO:0000313|EMBL:KLU69099.1};
RX PubMed=25284151; DOI=10.1016/j.cell.2014.09.008;
RA Seedorf H., Griffin N.W., Ridaura V.K., Reyes A., Cheng J., Rey F.E.,
RA Smith M.I., Simon G.M., Scheffrahn R.H., Woebken D., Spormann A.M.,
RA Van Treuren W., Ursell L.K., Pirrung M., Robbins-Pianka A., Cantarel B.L.,
RA Lombard V., Henrissat B., Knight R., Gordon J.I.;
RT "Bacteria from diverse habitats colonize and compete in the mouse gut.";
RL Cell 159:253-266(2014).
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 -!- 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 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLU69099.1}.
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DR EMBL; JNGB01000110; KLU69099.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1G0H4; -.
DR PATRIC; fig|1504536.3.peg.596; -.
DR Proteomes; UP000036477; Unassembled WGS sequence.
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 InterPro; IPR035090; Pyridoxal_P_attach_site.
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.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036477};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 658
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 818 AA; 94664 MW; C1B5E68F58445F2F CRC64;
MSKKFDKEAF INDVKANVKT LYRKTIDEAT KQQVFQAVSY TIKDTIIDNW LATQKQYETD
DPKTVYYMSM EFLMGRALGN NLINLTEYND VKDALEEIGF DLNVIEDEEP DAALGNGGLG
RLAACFLDSL ATLGYSSYGC GIRYRYGMFK QKIENGFQIE VPDNWLKDGN PFELRRPEYA
KEVKFGGYVR VVYDETTKRN RFIQEGCQSV RAIPFDIPIV GYDNRIVNTL RVWDAEAIND
FQLDSFDKGD YQKAVEQENL ARNIVEVLYP NDNHYAGKEL RLKQQYFFIS ASVQAAIEKY
KKKHSDMRKF HEKVTFQLND THPTVAVAEL MRILVDEENL EWDEAWEVTT KTCAYTNHTI
MAEALEKWPI ELFSRLLPRI YQIIEEINRR FLIEVGRKYP GDQNKVNKMA IIHDGQVKMA
HLAIVAGYSV NGVAQLHTEI LKKQELRDFY EMMPQKFNNK TNGITQRRFL LHANPLLAKW
VTAHIGDEWI TDLPQISKLK IYAEDKKAQQ EFMNIKYQNK VRLAGYILEH NGVEIDPRSI
FDVQVKRLHE YKRQLMNILH VMYLYNTIKD HPEMDFYPRT FIFGAKAAAG YRRAKLTIKL
INAVADVVNN DRSIKGKLKV VFIEDYRVSN AEWIFAASDV SEQISTASKE ASGTGNMKFM
LNGAPTLGTM DGANVEIVEE VGEENAFIFG LTADEVINFE NNGGYHPMDY FNNDQDIRRV
LMQLINGEYA KDDPERFREI YDSLLNTNSS DRADTYFILA DFKSYAEAQR RVEEAYRDET
RWAKMAILNV ASSGKFTSDR TIQQYVDEIW HLDKVVIE
//
