ID D4K9L3_9FIRM Unreviewed; 753 AA.
AC D4K9L3;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=FPR_12120 {ECO:0000313|EMBL:CBL01526.1};
OS Faecalibacterium prausnitzii SL3/3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Faecalibacterium.
OX NCBI_TaxID=657322 {ECO:0000313|EMBL:CBL01526.1, ECO:0000313|Proteomes:UP000007059};
RN [1] {ECO:0000313|EMBL:CBL01526.1, ECO:0000313|Proteomes:UP000007059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL3/3 {ECO:0000313|EMBL:CBL01526.1,
RC ECO:0000313|Proteomes:UP000007059};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Faecalibacterium prausnitzii SL3/3.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL01526.1, ECO:0000313|Proteomes:UP000007059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL3/3 {ECO:0000313|EMBL:CBL01526.1,
RC ECO:0000313|Proteomes:UP000007059};
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; FP929046; CBL01526.1; -; Genomic_DNA.
DR AlphaFoldDB; D4K9L3; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; fpa:FPR_12120; -.
DR PATRIC; fig|657322.3.peg.1106; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_9; -.
DR Proteomes; UP000007059; 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; 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 601
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 753 AA; 84160 MW; 4BB3741202FBF407 CRC64;
MSFTETLQSI TGKLLADCTD QELYLALLEL VRQKSADRVQ PVTGRKLYYI SAEFLIGKLL
SNNLINLGLY DEARSALAAA GKRLSDIEEV EPEPSLGNGG LGRLAACFLD SLATLNLPGD
GVGLRYHFGL FHQSFEDGVQ NEKPDPWLTA HSWAEKTDTT YPVELAGKEY TARLYKLAVT
GYEGRTNTLN LFDLDTIDES IVHDGIAFDK TAIDKNLTLF LYPDDSDEAG RRLRVYQQYL
MVSAGAQLIL AECAARGCNF HDLADYAAIQ INDTHPSMVI PELIRLLGER GIEFEEAVEI
VTKTCAYTNH TILAEALEKW PRAYLDAVVP QLMPIIEKLD ALARTRTEDE SLAIIDKDDR
VHMAHMDIHF THSTNGVAAL HTEILKNSEL HGFYELYPEK FNNKTNGITF RRWLLECDPR
LTATLEKHIG SGFRKDAAEL EKLLAFVDDE TVLSELTAVK KANKEALADW LLHTQKVTVN
TDAVFDIQSK RLHEYKRQQL NLLYLIHQYY EIKAGHLPAV PLVSIFGAKA APAYTIAKDI
IHALLTLSKV IAADPEVSKW LQVVFVENYN VTAAEKLIPA CDLSEQISLA SKEASGTGNM
KFMLNGALTL GTMDGANVEI SQQVGEENIY IFGQTSDQVI HRYAVGDYDP AQWVEGDANI
RRAISFLTGP EMLAAGHAEN LTRLHDELIH KDWFQTLPDF NAYVVRKGQA LSDYACDPTG
WRRKCLVNIA KAGMFSSDRT IAEYDRDIWH LGK
//
