ID D7GUG3_9FIRM Unreviewed; 829 AA.
AC D7GUG3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=CK3_18080 {ECO:0000313|EMBL:CBL41455.1};
OS butyrate-producing bacterium SS3/4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=245014 {ECO:0000313|EMBL:CBL41455.1, ECO:0000313|Proteomes:UP000008961};
RN [1] {ECO:0000313|EMBL:CBL41455.1, ECO:0000313|Proteomes:UP000008961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL41455.1,
RC ECO:0000313|Proteomes:UP000008961};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Clostridiales sp. SS3/4.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL41455.1, ECO:0000313|Proteomes:UP000008961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL41455.1,
RC ECO:0000313|Proteomes:UP000008961};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FP929062; CBL41455.1; -; Genomic_DNA.
DR AlphaFoldDB; D7GUG3; -.
DR KEGG; bprs:CK3_18080; -.
DR PATRIC; fig|245014.3.peg.210; -.
DR HOGENOM; CLU_010198_1_1_9; -.
DR BioCyc; BBAC245014:G1314-1544-MONOMER; -.
DR Proteomes; UP000008961; 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 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 667
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 829 AA; 95896 MW; A032051D988F491E CRC64;
MQGIIMKEDL GVSQTMNKDE LKKVIALNVK SLYRKTIDEA TPAMIYQAVA LAVKDMIIDR
WIATHKEYEK QDAKVVYYMS MEFLTGRFLG NNIISLCEQK EIEEALSELG FDLNSIEDQE
RDPALGNGGL GRLAACFLDS LASLGYPAYG CGIRYRYGMF KQQIRDGYQI EVPDEWLKDG
YPFEIRRAEY ATEVKFGGYV ETEWDGKRNH FVQKGYQSVM AVPYDIPIVG YGNNVVNSLR
IWDAQPVNTF NLSEFDKGDY QKAVEQENLA KTIVEVLYPN DNHYSGKELR LKQQYFFISA
SVQRAIKKYK EKHDDIHKFY EKASFQLNDT HPTVAVAELM RILLDEENLE WDEAWEITTK
TCAYTNHTIM AEALEKWPIE LFSRLLPRVY QIVEEINRRF VAQIQQRYPG DNEKIRRMAI
IYDGQVRMAY LAIVGSFSVN GVAKLHTEIL EKQELRDFYE MMPEKFNNKT NGITQRRFLL
HGNPLLADWV TDKIGNEWIT DLSNIKKLSV YVDDEKCQQE FMNIKYQNKI RLAKYIKEHN
GIDVDPRSIF DVQVKRLHEY KRQLMNILHV MYLYNQLKDN PNMDIVPRTF IFGAKAAAGY
KRAKLTIKLI NNVADVINND KSIGGKLKVV FIEDYRVSNA ELIFSAADVS EQISTASKEA
SGTGNMKFML NGALTIGTMD GANVEMAEEV GKENMFIFGA SADEIINLEN NGGYNPMDIF
NNDQDIRRVL MQLINGYYSP QDPELFRDIY NSLLNTQSSD RADTYFILKD FRSYAEAHRK
IDQAYRDEKW WARTAMLNTA SAGKFSSDRT IEEYVRDIWH LKKIKVELK
//
