ID A0A3D0CLG9_9LACT Unreviewed; 761 AA. AC A0A3D0CLG9; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 31-JUL-2019, entry version 6. 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; Firmicutes; 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 RT substantially revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). CC -!- FUNCTION: Phosphorylase is an important allosteric enzyme in CC carbohydrate metabolism. Enzymes from different sources differ in CC their regulatory mechanisms and in their natural substrates. CC However, all known phosphorylases share catalytic and structural CC properties. {ECO:0000256|RuleBase:RU000587}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha- CC D-glucosyl](n-1) + alpha-D-glucose 1-phosphate; CC Xref=Rhea:RHEA:41732, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, CC ChEBI:CHEBI:15444, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; CC EC=2.4.1.1; Evidence={ECO:0000256|RuleBase:RU000587}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|RuleBase:RU000587}; CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family. CC {ECO:0000256|RuleBase:RU000587}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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 CDD; cd04300; GT35_Glycogen_Phosphorylase; 1. DR InterPro; IPR011833; Glycg_phsphrylas. DR InterPro; IPR000811; Glyco_trans_35. DR InterPro; IPR035090; Pyridoxal_P_attach_site. DR PANTHER; PTHR11468; PTHR11468; 1. DR Pfam; PF00343; Phosphorylase; 1. DR PIRSF; PIRSF000460; Pprylas_GlgP; 1. DR TIGRFAMs; TIGR02093; P_ylase; 1. DR PROSITE; PS00102; PHOSPHORYLASE; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000262242}; KW Glycosyltransferase {ECO:0000256|RuleBase:RU000587}; KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1, KW ECO:0000256|RuleBase:RU000587}; KW Transferase {ECO:0000256|RuleBase:RU000587}. FT COILED 326 346 {ECO:0000256|SAM:Coils}. FT MOD_RES 605 605 N6-(pyridoxal phosphate)lysine. FT {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 //