ID A8RFI4_9FIRM Unreviewed; 804 AA.
AC A8RFI4;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 64.
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:EDP10237.1};
GN ORFNames=EUBDOL_02251 {ECO:0000313|EMBL:EDP10237.1};
OS Amedibacillus dolichus DSM 3991.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Amedibacillus.
OX NCBI_TaxID=428127 {ECO:0000313|EMBL:EDP10237.1, ECO:0000313|Proteomes:UP000004090};
RN [1] {ECO:0000313|EMBL:EDP10237.1, ECO:0000313|Proteomes:UP000004090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3991 {ECO:0000313|EMBL:EDP10237.1,
RC ECO:0000313|Proteomes:UP000004090};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Eubacterium dolichum (DSM 3991).";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDP10237.1, ECO:0000313|Proteomes:UP000004090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3991 {ECO:0000313|EMBL:EDP10237.1,
RC ECO:0000313|Proteomes:UP000004090};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2007) 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}.
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:EDP10237.1}.
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DR EMBL; ABAW02000025; EDP10237.1; -; Genomic_DNA.
DR RefSeq; WP_004800883.1; NZ_DS483478.1.
DR AlphaFoldDB; A8RFI4; -.
DR STRING; 428127.EUBDOL_02251; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR GeneID; 83059619; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_9; -.
DR Proteomes; UP000004090; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 650
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 804 AA; 92983 MW; A287612246C7BC23 CRC64;
MANEFKNKDE FIKEFKKRII RHFGCSIERA HITEKYMILG EMVRDHASEN WNLTKDVISE
KQEKQMYYFS MEFLMGRLLT NNLMNLGIYD IVKEGLDELG IDINELEEME SDAGLGNGGL
GRLAACFLDS LASLNLAGHG NCIRYEYGLF KQKIEHNEQV EVPDKWLSLG NVWEVRKPKH
SVDVKFGGRV EMWMGEDGKA VVNHIPSLVV RAVPYDMPII GQNTATTNTL RLWSAEVADD
ACDASSLNEY VNEVREICRN VYPDDSTEHG KLLRLKQQYF FVSAGIYNII ESHLRTYGSL
DNFADKVAIQ LNDTHPVLCI PELMRILLDE YRFEWDDAWE MTKKTMAYTN HTVLSEALEK
WPVQYVRELL PRIYMIIEEI DNRFKYHLSH DFGRPDLIDS CAIIKEGQVH MAHLAIVGSH
SVNGVAALHT RILKEDVMKS FYELYPEKFN NKTNGITHRR WLLHSNPQLT DLLEKTIGPQ
FKTNPDKLTD LMQYVDDEKL QTQFMEVKLE RKKILADYIK KTLNIEVDIH SIFDVQAKRL
HAYKRQLLNI LNIMDLYFRM KNDSNYRIYP RTFIFAAKAA PSYTFAKEVI KLIHCVADKV
NNDPEISKYM KVVFIPNYGV SIAEILMNAA DVSEQISTAG KEASGTGNMK FMMNGAITLG
TMDGANVEIV ERVGFENAEI FGLRADDVAL IRRENSYDVW RKYHENANIH RIIDALTDGT
FSSNPNDFKL IYNELMFKND EYLLLADYDA YAHARTNIER RYQDKRGWAK MCLINIAQSA
FFSSDRTIRQ YAEEIWNLKA VELD
//
