ID R4R368_9SOLA Unreviewed; 361 AA. AC R4R368; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 25-OCT-2017, entry version 12. DE RecName: Full=Phosphoglycerate kinase {ECO:0000256|RuleBase:RU000532}; DE EC=2.7.2.3 {ECO:0000256|RuleBase:RU000532}; DE Flags: Fragment; GN Name=PGK {ECO:0000313|EMBL:AGL76992.1}; OS Anisodus luridus. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae; OC Hyoscyameae; Anisodus. OX NCBI_TaxID=258458 {ECO:0000313|EMBL:AGL76992.1}; RN [1] {ECO:0000313|EMBL:AGL76992.1} RP NUCLEOTIDE SEQUENCE. RA Qin B., Ma L., Liao Z.; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + 3-phospho-D-glycerate = ADP + 3-phospho- CC D-glyceroyl phosphate. {ECO:0000256|RuleBase:RU000532}. CC -!- SUBUNIT: Monomer. {ECO:0000256|RuleBase:RU000696}. CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family. CC {ECO:0000256|RuleBase:RU000532}. 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; KC713803; AGL76992.1; -; mRNA. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:InterPro. DR CDD; cd00318; Phosphoglycerate_kinase; 1. DR Gene3D; 3.40.50.1260; -; 2. DR HAMAP; MF_00145; Phosphoglyc_kinase; 1. DR InterPro; IPR001576; Phosphoglycerate_kinase. DR InterPro; IPR015911; Phosphoglycerate_kinase_CS. DR InterPro; IPR015824; Phosphoglycerate_kinase_N. DR InterPro; IPR036043; Phosphoglycerate_kinase_sf. DR PANTHER; PTHR11406; PTHR11406; 1. DR Pfam; PF00162; PGK; 1. DR PIRSF; PIRSF000724; Pgk; 1. DR PRINTS; PR00477; PHGLYCKINASE. DR SUPFAM; SSF53748; SSF53748; 1. DR PROSITE; PS00111; PGLYCERATE_KINASE; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|PIRSR:PIRSR000724-2}; KW Kinase {ECO:0000256|RuleBase:RU000532, ECO:0000313|EMBL:AGL76992.1}; KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000724-2}; KW Transferase {ECO:0000256|RuleBase:RU000532, KW ECO:0000313|EMBL:AGL76992.1}. FT NP_BIND 342 345 ATP. {ECO:0000256|PIRSR:PIRSR000724-2}. FT REGION 10 12 Substrate binding. {ECO:0000256|PIRSR: FT PIRSR000724-1}. FT REGION 49 52 Substrate binding. {ECO:0000256|PIRSR: FT PIRSR000724-1}. FT BINDING 26 26 Substrate. {ECO:0000256|PIRSR: FT PIRSR000724-1}. FT BINDING 107 107 Substrate. {ECO:0000256|PIRSR: FT PIRSR000724-1}. FT BINDING 140 140 Substrate. {ECO:0000256|PIRSR: FT PIRSR000724-1}. FT BINDING 191 191 ATP. {ECO:0000256|PIRSR:PIRSR000724-2}. FT BINDING 313 313 ATP. {ECO:0000256|PIRSR:PIRSR000724-2}. FT NON_TER 1 1 {ECO:0000313|EMBL:AGL76992.1}. FT NON_TER 361 361 {ECO:0000313|EMBL:AGL76992.1}. SQ SEQUENCE 361 AA; 38505 MW; DE9149DBCBE9DFAF CRC64; KGKRVFVRVD LNVPLDDNFN ITDDTRIRAA LPTINYLMQN GARVILASHL GRPKGVTPKY SLKPLVPRLS ELLGLEVKMA NDSVGPEVEK LVAELPEGGV LLLENVRFYK EEEKNEPEFA KKLASLADLY VNDAFGTAHR AHASTEGVAK VLKPAVAGFL MQKELDYLVG AVSNPQKPFA AIVGGSEVSS KIGVIESLLE KVDVLLLGGG MIFTFYKAQG YAVGSSLVEE DKLDLATSLM EKAKTKGVSL LLPTDVVIAD KFAADANSKI VPASEIPDDW MGLDIGPDAI KSFGSALDTT KTIIWNGPMG VFEFDKFAAG TEAIAHKLAE LSGKGVTTII GGGDSVAAVE KVGLAEKMSH I //