ID   R4R368_9SOLA            Unreviewed;       361 AA.
AC   R4R368;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   16-JAN-2019, entry version 14.
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:
CC       Reaction=3-phospho-D-glycerate + ATP = 3-phospho-D-glyceroyl
CC         phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216;
CC         EC=2.7.2.3; Evidence={ECO:0000256|RuleBase:RU000532};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|RuleBase:RU000696}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000256|RuleBase:RU000532}.
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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
//