ID A0A3D0CLG9_9LACT Unreviewed; 761 AA. AC A0A3D0CLG9; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 03-MAY-2023, entry version 16. DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587}; DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587}; GN ORFNames=DEO37_10435 {ECO:0000313|EMBL:HBY90837.1}; OS Aerococcaceae bacterium. OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae. OX NCBI_TaxID=2053495 {ECO:0000313|EMBL:HBY90837.1, ECO:0000313|Proteomes:UP000262242}; RN [1] {ECO:0000313|EMBL:HBY90837.1, ECO:0000313|Proteomes:UP000262242} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UBA11280 {ECO:0000313|EMBL:HBY90837.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny substantially RT revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). 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:HBY90837.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DOTN01000071; HBY90837.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3D0CLG9; -. DR EnsemblBacteria; HBY90837; HBY90837; DEO37_10435. DR Proteomes; UP000262242; 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 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 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 TIGRFAMs; TIGR02093; P_ylase; 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 605 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1" SQ SEQUENCE 761 AA; 87833 MW; 58C15EC151053EC3 CRC64; MSILENYVLD NFDKPIRECS DQEMYKVLLD LVRDKSRELP TNDDKKKKLY YFSAEFLIGK LLSNNLLNLG IYDEVNNELI ANGKNIMDIE QAELEPSLGN GGLGRLAACF VDSITTLGIN GDGVGLNYHF GLFKQVFKDN QQTQLPDPWI TEESWLIKNE KSYEVPFNNF TLKSTLYDID VLGYNSDTRN RLRLFDLDSV TSDIIEEGTI HFDKTNIEEN LTLFLYPDDS DREGELLRIF QQYYMVSNGA QLILDEAVAR GSNLHDLAEY AVIQINDTHP AFVIPEMIRL LTQRGIDFDE AIQITQTMTA FTNHTILAEA LEKWPIDELE QVMPEIANII RELDNRKKDE FPNNHAVSII DEHDRVHMAH MAIHYGYSIN GVAALHTEIL KNSELKAFFD IYPNKFINKT NGITFRRWIM DANKELADFI DDLISDEWRT SANLEPLLDF KDDENVLTKL RAIKFNNKQR LSHRLETMQN VTINEHSIID VHIKRIHEYK RQQMLLLYII HKYNDIKNGN IPKTPITIIF GGKAAAAYTI ARDIIHAILT VSEIIANDDE VNEHFQVVMV ENYNVTHAQY LIPATDISEQ ISLASKEASG TGNMKFMLNG ALTLCTLDGA NVEIADLVGE ENIYIFGKRS EEIVDLYATN GYNARSYYER ETIKPLVDFL MDPKMLELGD EGRLSRLHYD MINKDYFMAL IDLEEFIEIK EKVYEDYEDH DTWTRKALIN IAKAGFFSSD RTINEYNRDI WHLEQEIKNV N //