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 31-JAN-2018, entry version 30. DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587}; DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587}; GN ORFNames=CR079_19515 {ECO:0000313|EMBL:PHM96857.1}, CR080_06270 GN {ECO:0000313|EMBL:PHM94144.1}, CR081_07870 GN {ECO:0000313|EMBL:PHK78529.1}, CR082_20425 GN {ECO:0000313|EMBL:PHK80957.1}, CR083_05460 GN {ECO:0000313|EMBL:PHK89063.1}, CR084_00800 GN {ECO:0000313|EMBL:PHP39532.1}, CR085_00280 GN {ECO:0000313|EMBL:PHP34436.1}, CR086_09530 GN {ECO:0000313|EMBL:PHP62468.1}, CS350_07035 GN {ECO:0000313|EMBL:PHZ89873.1}, CTI29_01625 GN {ECO:0000313|EMBL:ATU58679.1}, DD95_06320 GN {ECO:0000313|EMBL:KTZ14029.1}; OS Salmonella typhimurium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=90371 {ECO:0000313|EMBL:KTZ14029.1, ECO:0000313|Proteomes:UP000054461}; 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|Proteomes:UP000221873, ECO:0000313|Proteomes:UP000222775, ECO:0000313|Proteomes:UP000223380} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SE368 {ECO:0000313|EMBL:PHM96857.1, RC ECO:0000313|Proteomes:UP000222775}, SE373 RC {ECO:0000313|EMBL:PHM94144.1, ECO:0000313|Proteomes:UP000221873}, RC SE376 {ECO:0000313|EMBL:PHK78529.1, RC ECO:0000313|Proteomes:UP000225473}, SE389 RC {ECO:0000313|EMBL:PHK80957.1, ECO:0000313|Proteomes:UP000224379}, RC SE426 {ECO:0000313|EMBL:PHK89063.1, RC ECO:0000313|Proteomes:UP000223380}, SE484 RC {ECO:0000313|EMBL:PHP39532.1, ECO:0000313|Proteomes:UP000226254}, RC SE492 {ECO:0000313|EMBL:PHP34436.1, RC ECO:0000313|Proteomes:UP000224064}, and SE494 RC {ECO:0000313|EMBL:PHP62468.1, ECO:0000313|Proteomes:UP000223987}; RA Sanad Y., Khajanchi B., Deck J., Cox J., Thaker R., Han J., Nayak R., RA Foley S.; RT "Characterization of the Virulence Potential of Salmonella enterica RT Isolates Carrying Incompatibility Group FIB Plasmids using Caco-2 RT Intestinal Epithelial Cells."; RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:PHZ89873.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CFSAN070646 {ECO:0000313|EMBL:PHZ89873.1}; RA Hoffmann M., Timme R., Sanchez M., Binet R.; RT "Construction of stable fluorescent laboratory control strains."; RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:ATU58679.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BL10 {ECO:0000313|EMBL:ATU58679.1}; RA Banno H., Chua N.-H.; RL Submitted (OCT-2017) 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:RU000587}. 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; CP024619; ATU58679.1; -; Genomic_DNA. DR EMBL; JYVU01000013; KTZ14029.1; -; Genomic_DNA. DR EMBL; PDNM01000004; PHK78529.1; -; Genomic_DNA. DR EMBL; PDNL01000029; PHK80957.1; -; Genomic_DNA. DR EMBL; PDNK01000014; PHK89063.1; -; Genomic_DNA. DR EMBL; PDNN01000010; PHM94144.1; -; Genomic_DNA. DR EMBL; PDNO01000027; PHM96857.1; -; Genomic_DNA. DR EMBL; PDOJ01000001; PHP34436.1; -; Genomic_DNA. DR EMBL; PDOI01000003; PHP39532.1; -; Genomic_DNA. DR EMBL; PDOK01000007; PHP62468.1; -; Genomic_DNA. DR EMBL; PEHQ01000003; PHZ89873.1; -; Genomic_DNA. DR RefSeq; WP_000993428.1; NZ_PEHQ01000003.1. DR EnsemblBacteria; KKE12239; KKE12239; TJ44_21595. DR EnsemblBacteria; KTZ14029; KTZ14029; DD95_06320. DR KEGG; seni:CY43_18360; -. DR PATRIC; fig|90371.1185.peg.3832; -. DR KO; K00688; -. DR Proteomes; UP000054461; Unassembled WGS sequence. DR Proteomes; UP000221873; Unassembled WGS sequence. DR Proteomes; UP000222775; Unassembled WGS sequence. DR Proteomes; UP000223380; Unassembled WGS sequence. DR Proteomes; UP000223987; Unassembled WGS sequence. DR Proteomes; UP000224064; Unassembled WGS sequence. DR Proteomes; UP000224379; Unassembled WGS sequence. DR Proteomes; UP000225473; Unassembled WGS sequence. DR Proteomes; UP000226254; 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; GT1_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 Complete proteome {ECO:0000313|Proteomes:UP000054461, KW ECO:0000313|Proteomes:UP000221873, ECO:0000313|Proteomes:UP000222775, KW ECO:0000313|Proteomes:UP000223380}; 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 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 //