ID A0A0D6I812_SALTM Unreviewed; 815 AA. AC A0A0D6I812; A0A0M2J527; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 02-NOV-2016, 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 Name=glgP {ECO:0000313|EMBL:CKH84803.1}; GN ORFNames=DD95_06320 {ECO:0000313|EMBL:KTZ14029.1}, ERS450001_03709 GN {ECO:0000313|EMBL:CKH84803.1}, TJ44_21595 GN {ECO:0000313|EMBL:KKE12239.1}; OS Salmonella typhimurium. OG Plasmid 2 {ECO:0000313|EMBL:CKH84803.1}. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=90371 {ECO:0000313|EMBL:CKH84803.1}; RN [1] {ECO:0000313|EMBL:KTZ14029.1, ECO:0000313|Proteomes:UP000054461} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CVM N32045 {ECO:0000313|EMBL:KTZ14029.1, RC ECO:0000313|Proteomes:UP000054461}; RA Chen Y., Folster J., Ayers S., Kabera C., Li C., Mukherjee S., Lam C., RA Zhao S., McDermott P.; RT "Salmonella Genotype and Phenotype Association."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CKH84803.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCTC13348 {ECO:0000313|EMBL:CKH84803.1}; RC PLASMID=2 {ECO:0000313|EMBL:CKH84803.1}; RA Informatics Pathogen; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:KKE12239.1, ECO:0000313|Proteomes:UP000034436} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ABBSB1189-1 {ECO:0000313|EMBL:KKE12239.1, RC ECO:0000313|Proteomes:UP000034436}; RA Murphy D.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. 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: ((1->4)-alpha-D-glucosyl)(n) + phosphate = CC ((1->4)-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate. CC {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:RU004179}. 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; LN829402; CKH84803.1; -; Genomic_DNA. DR EMBL; LAPF01000001; KKE12239.1; -; Genomic_DNA. DR EMBL; JYVU01000013; KTZ14029.1; -; Genomic_DNA. DR RefSeq; WP_000993428.1; NZ_MATL01000010.1. DR EnsemblBacteria; KKE12239; KKE12239; TJ44_21595. DR EnsemblBacteria; KLT11990; KLT11990; ABT69_22320. DR EnsemblBacteria; KLT23827; KLT23827; ABT85_22345. DR EnsemblBacteria; KLT24717; KLT24717; ABT82_22390. DR EnsemblBacteria; KLT25918; KLT25918; ABT80_22285. DR EnsemblBacteria; KLT35658; KLT35658; ABT86_22365. DR EnsemblBacteria; KMJ17912; KMJ17912; ABT70_22325. DR EnsemblBacteria; KMJ19010; KMJ19010; ABT77_22405. DR EnsemblBacteria; KMJ25351; KMJ25351; ABT73_17995. DR EnsemblBacteria; KMJ33273; KMJ33273; ABT75_18060. DR EnsemblBacteria; KMJ34320; KMJ34320; ABT76_22245. DR EnsemblBacteria; KMJ36185; KMJ36185; ABT74_22375. DR EnsemblBacteria; KMJ61402; KMJ61402; ABT91_22320. DR EnsemblBacteria; KMJ74619; KMJ74619; ABT89_22305. DR EnsemblBacteria; KMJ77482; KMJ77482; ABT87_22320. DR EnsemblBacteria; KMM48493; KMM48493; ABT68_22430. DR EnsemblBacteria; KTZ14029; KTZ14029; DD95_06320. DR KEGG; seni:CY43_18360; -. DR KO; K00688; -. DR Proteomes; UP000034436; Unassembled WGS sequence. DR Proteomes; UP000054461; Unassembled WGS sequence. DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR CDD; cd04300; GT1_Glycogen_Phosphorylase; 1. DR InterPro; IPR011833; Glycg_phsphrylas. DR InterPro; IPR000811; Glyco_trans_35. 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 Complete proteome {ECO:0000313|Proteomes:UP000034436, KW ECO:0000313|Proteomes:UP000054461}; KW Glycosyltransferase {ECO:0000256|RuleBase:RU000587, KW ECO:0000313|EMBL:CKH84803.1}; Plasmid {ECO:0000313|EMBL:CKH84803.1}; KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1, KW ECO:0000256|RuleBase:RU000587}; KW Transferase {ECO:0000256|RuleBase:RU000587, KW ECO:0000313|EMBL:CKH84803.1}. FT MOD_RES 662 662 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|PIRSR:PIRSR000460-1}. SQ SEQUENCE 815 AA; 93343 MW; 4464A9CBB044F1C2 CRC64; MNAPFTYASP TLSVEALKHS IAYKLMFTIG KDPVIANKHE WLNATLFAVR DRLVERWLRS NRAQLSQETR QVYYLSMEFL IGRTLSNALL SLGIYDDVKG ALEAMGLDLE ELIDEENDPG LGNGGLGRLA ACFLDSLATL GLPGRGYGIR YDYGMFKQNI VDGRQKESPD YWLEYGNPWE FKRHNTRYKV LFGGRIQQEG KKARWIETEE ILAVAYDQII PGYDTDATNT LRLWNAQASS EINLGKFNQG DYFAAVEDKN HSENVSRVLY PDDSTYSGRE LRLRQEYFLV SATVQDILHR HYQLHKTYEN LADKIAIHLN DTHPVLSIPE LMRLLIDEHK FSWDDAFEVC CQVFSYTNHT LMSEALETWP VDMLGKILPR HLQIIFEIND YFLKTVQEQY PNDTSLLGRA SIIDESNGRR VRMAWLAVVV SHKVNGVSEL HSNLMVQSLF ADFAKIFPTR FCNVTNGVTP RRWLALANPP LSDVLDENIG RTWRTDLSQL SELKQHCDYP LVNHAVRQAK LENKKRLAVV IAQQLNVVVN PKALFDVQIK RIHEYKRQLM NVLHVITRYN RIKENPEADW VPRVNIFAGK AASAYYMAKH IIHLINDVAK VINNDPQIGD KLKVVFIPNY SVSLAQVIIP AADLSEQISL AGTEASGTSN MKFALNGALT IGTLDGANVE MQEHIGEENI FIFGNTAEEV EALRRQGYKP RDYYEKDEEL HQVLTQIGSG VFNPEEPGRY RDLVDSLINF GDHYQVLADY RSYVDCQDKV DELYRRPEEW TTKAMLNIAN MGYFSSDRTI KEYAENIWHI DPVRL //