ID A0A0D6I812_SALTM Unreviewed; 815 AA. AC A0A0D6I812; A0A0F7JDZ3; A0A0M2J527; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 24-JUL-2024, entry version 72. DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587}; DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587}; GN Name=malP_2 {ECO:0000313|EMBL:AKH09164.1}; GN ORFNames=AAB27_04095 {ECO:0000313|EMBL:ECV8760070.1}, AU613_00860 GN {ECO:0000313|EMBL:MIT47449.1}, AVC05_05565 GN {ECO:0000313|EMBL:ECY5340711.1}, B1P38_08895 GN {ECO:0000313|EMBL:ECU8353703.1}, CE70_05985 GN {ECO:0000313|EMBL:ECE0294748.1}, CFF59_07650 GN {ECO:0000313|EMBL:EDI6665133.1}, CVR97_05625 GN {ECO:0000313|EMBL:PJH62883.1}, DD95_06320 GN {ECO:0000313|EMBL:KTZ14029.1}, DMO92_12640 GN {ECO:0000313|EMBL:EBU9272898.1}, DPF41_07460 GN {ECO:0000313|EMBL:EBW3627930.1}, DPS76_12155 GN {ECO:0000313|EMBL:EBW5463193.1}, DRM14_11880 GN {ECO:0000313|EMBL:MLP86011.1}, DU071_02150 GN {ECO:0000313|EMBL:EBY1700767.1}, E0935_01465 GN {ECO:0000313|EMBL:ECF1541925.1}, EER35_04655 GN {ECO:0000313|EMBL:EBZ6920280.1}, F3R12_10560 GN {ECO:0000313|EMBL:ECW0640286.1}, G0J40_08680 GN {ECO:0000313|EMBL:HAC9070190.1}, GB466_14350 GN {ECO:0000313|EMBL:HAB0971733.1}, SE14_03748 GN {ECO:0000313|EMBL:AKH09164.1}; OS Salmonella typhimurium. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=90371 {ECO:0000313|EMBL:HAC9070190.1}; 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:AKH09164.1, ECO:0000313|Proteomes:UP000034636} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YU39 {ECO:0000313|EMBL:AKH09164.1, RC ECO:0000313|Proteomes:UP000034636}; RX PubMed=26089426; RA Calva E., Silva C., Zaidi M.B., Sanchez-Flores A., Estrada K., Silva G.G., RA Soto-Jimenez L.M., Wiesner M., Fernandez-Mora M., Edwards R.A., Vinuesa P.; RT "Complete Genome Sequencing of a Multidrug-Resistant and Human-Invasive RT Salmonella enterica Serovar Typhimurium Strain of the Emerging Sequence RT Type 213 Genotype."; RL Genome Announc. 3:e00663-15(2015). RN [3] {ECO:0000313|EMBL:PJH62883.1, ECO:0000313|Proteomes:UP000228538} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=N029 {ECO:0000313|EMBL:PJH62883.1, RC ECO:0000313|Proteomes:UP000228538}; 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 (NOV-2017) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:HAC9070190.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=S04006-14 {ECO:0000313|EMBL:HAC9070190.1}, and Salmonella RC enterica {ECO:0000313|EMBL:HAB0971733.1}; RX PubMed=30286803; DOI=10.1186/s13059-018-1540-z; RA Souvorov A., Agarwala R., Lipman D.J.; RT "SKESA: strategic k-mer extension for scrupulous assemblies."; RL Genome Biol. 19:153-153(2018). RN [5] {ECO:0000313|EMBL:ECE0294748.1, ECO:0000313|Proteomes:UP000338496} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AUSMDU00020735 {ECO:0000313|EMBL:ECW0640286.1}, and RC VA_WGS-00080 {ECO:0000313|EMBL:ECE0294748.1, RC ECO:0000313|Proteomes:UP000338496}; RG GenomeTrakr network: Whole genome sequencing for foodborne pathogen traceback; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:EDI6665133.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PNUSAS008736 {ECO:0000313|EMBL:ECU8353703.1}, and PNUSAS016739 RC {ECO:0000313|EMBL:EDI6665133.1}; RG PulseNet: The National Subtyping Network for Foodborne Disease Surveillance; RA Tarr C.L., Trees E., Katz L.S., Carleton-Romer H.A., Stroika S., RA Kucerova Z., Roache K.F., Sabol A.L., Besser J., Gerner-Smidt P.; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:EBY1700767.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=231108 {ECO:0000313|EMBL:EBW3627930.1}, 265852 RC {ECO:0000313|EMBL:ECF1541925.1}, 29290 {ECO:0000313|EMBL:MIT47449.1}, RC 356083 {ECO:0000313|EMBL:EBY1700767.1}, 422529 RC {ECO:0000313|EMBL:EBW5463193.1}, 425567 {ECO:0000313|EMBL:MLP86011.1}, RC 43916 {ECO:0000313|EMBL:ECY5340711.1}, 488670 RC {ECO:0000313|EMBL:EBU9272898.1}, 632340 RC {ECO:0000313|EMBL:EBZ6920280.1}, and 86846 RC {ECO:0000313|EMBL:ECV8760070.1}; RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|EMBL:HAC9070190.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=S04006-14 {ECO:0000313|EMBL:HAC9070190.1}, and Salmonella RC enterica {ECO:0000313|EMBL:HAB0971733.1}; RG NCBI Pathogen Detection Project; RL Submitted (JAN-2019) 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 --------------------------------------------------------------------------- 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; CP011428; AKH09164.1; -; Genomic_DNA. DR EMBL; AAHDPU010000009; EBU9272898.1; -; Genomic_DNA. DR EMBL; AAHIDF010000006; EBW3627930.1; -; Genomic_DNA. DR EMBL; AAHIPE010000011; EBW5463193.1; -; Genomic_DNA. DR EMBL; AAHNIA010000002; EBY1700767.1; -; Genomic_DNA. DR EMBL; AAHRYM010000003; EBZ6920280.1; -; Genomic_DNA. DR EMBL; AAIGQE010000003; ECE0294748.1; -; Genomic_DNA. DR EMBL; AAIKGB010000001; ECF1541925.1; -; Genomic_DNA. DR EMBL; AAKRET010000007; ECU8353703.1; -; Genomic_DNA. DR EMBL; AAKUOT010000005; ECV8760070.1; -; Genomic_DNA. DR EMBL; AAKVET010000005; ECW0640286.1; -; Genomic_DNA. DR EMBL; AALDNI010000008; ECY5340711.1; -; Genomic_DNA. DR EMBL; AAMLUT010000005; EDI6665133.1; -; Genomic_DNA. DR EMBL; DAAFPQ010000010; HAB0971733.1; -; Genomic_DNA. DR EMBL; DAANAV010000004; HAC9070190.1; -; Genomic_DNA. DR EMBL; JYVU01000013; KTZ14029.1; -; Genomic_DNA. DR EMBL; RSUA01000001; MIT47449.1; -; Genomic_DNA. DR EMBL; RVDJ01000010; MLP86011.1; -; Genomic_DNA. DR EMBL; PHGX01000020; PJH62883.1; -; Genomic_DNA. DR RefSeq; WP_000993428.1; NZ_WXYU01000002.1. DR AlphaFoldDB; A0A0D6I812; -. DR KEGG; seni:CY43_18360; -. DR PATRIC; fig|59201.135.peg.2884; -. DR eggNOG; COG0058; Bacteria. DR OMA; WLKQANP; -. DR Proteomes; UP000034636; Chromosome. DR Proteomes; UP000054461; Unassembled WGS sequence. DR Proteomes; UP000228538; Unassembled WGS sequence. DR Proteomes; UP000338496; Unassembled WGS sequence. DR Proteomes; UP000839581; Unassembled WGS sequence. DR Proteomes; UP000839595; Unassembled WGS sequence. DR Proteomes; UP000839616; Unassembled WGS sequence. DR Proteomes; UP000839617; Unassembled WGS sequence. DR Proteomes; UP000839905; Unassembled WGS sequence. DR Proteomes; UP000839907; Unassembled WGS sequence. DR Proteomes; UP000839908; Unassembled WGS sequence. DR Proteomes; UP000839909; Unassembled WGS sequence. DR Proteomes; UP000839911; Unassembled WGS sequence. DR Proteomes; UP000839914; Unassembled WGS sequence. DR Proteomes; UP000839915; Unassembled WGS sequence. DR Proteomes; UP000885258; Unassembled WGS sequence. DR Proteomes; UP000885385; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. 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:0005980; P:glycogen catabolic process; IEA:TreeGrafter. 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 662 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="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 //