ID   A0A0E0M833_ORYPU        Unreviewed;       971 AA.
AC   A0A0E0M833;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Phosphoglycerate kinase {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
DE            EC=2.7.2.3 {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
OS   Oryza punctata (Red rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC10G09790.3};
RN   [1] {ECO:0000313|EnsemblPlants:OPUNC10G09790.3}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OPUNC10G09790.3}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC         phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC         Evidence={ECO:0000256|RuleBase:RU000532};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|RuleBase:RU000696}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000256|ARBA:ARBA00008982, ECO:0000256|RuleBase:RU000532}.
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DR   AlphaFoldDB; A0A0E0M833; -.
DR   EnsemblPlants; OPUNC10G09790.3; OPUNC10G09790.3; OPUNC10G09790.
DR   Gramene; OPUNC10G09790.3; OPUNC10G09790.3; OPUNC10G09790.
DR   HOGENOM; CLU_008500_1_0_1; -.
DR   Proteomes; UP000026962; Chromosome 10.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 2.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR   InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb.
DR   PANTHER; PTHR11406; PHOSPHOGLYCERATE KINASE; 1.
DR   PANTHER; PTHR11406:SF32; PHOSPHOGLYCERATE KINASE; 1.
DR   Pfam; PF02390; Methyltransf_4; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51625; SAM_MT_TRMB; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000532};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532}.
FT   REGION          1..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          813..857
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          892..955
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        815..853
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        904..922
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        924..941
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   971 AA;  105100 MW;  A50CEBEC7F963DA5 CRC64;
     MYTSSIRATP RHASRNVSAS SHHIIRPDPK SATPYPRWLP LRNGTEADNS SPRRASRSRT
     PPPRREASGS ASSSSSTGRD GGGWPRGSVR ANGSGAAAGK FSGASASVRG TRKDGLMQKA
     CSVQLLRPSR SLRRESWPQS GGSVDKYSCI DRSTSYLYVQ SVRDFPIEKL NGEVVLVRLD
     SQLLCNPLGP CSLSLERTVS TIKYLYKAGA KVFLVTSWTP VLRSVNPVLK STETFADYMS
     SLLQVKVVPV NGVPGLTSFK PEEWMRNDII LFENLLNFKG ETANCNDFSQ KLASGAAIFV
     NDSFSLSHKM LASTVGITRF CHASLAGFHF EEELMQLRKI TDTTRRPFIA IIGGSNFLGK
     APALNLLASL CDGLFFVGKL SLQIMNGFGI PVPSCFVEKN ATKEVLQLIE TAHNRNIPIY
     YPTDTWCLNN KNNNHEKLEI LNSAELLPGW TPADIGPSTL EKISSLIPLY KKVLWIGPTG
     FDLTEEFSGG ATQLGRLLDK ASHNSCDIIL VGSAACKAVK GISGSSSKYT TFKNASVVLE
     FLKGKILPGV AALDKSYPYQ IPWNAIFSDS SQPLVVDIGS GNGLFLFQMA KNWEGSNFLG
     LEMNKKLVVR CLRDVASVDK RNLYFVSTNA TSTFRSILSS YPGHLALVTI QCPNPDFNKE
     QNRWRMVRRM LVEAIADLLQ PNGKSDVESV LFGMKEQFMT YGKGRLVVDG DGGGGHQMDN
     PFGAASDWER HVLARGAPMY RTMLSKSPMS ETVATLIADD RRTDHAPKTF WCVSMAASML
     NVTYVGGSSG SGALPSRYCI TCRMLGLAAG DGCRHSTSTK RSSSSAPATA SSSSSSSIGL
     LPQVTSRRNA PKANTSERVV ALPERTISGA KYPMVPTTCV VCGSSPPGVT VAMPSSASAA
     PPNPSYTNPT PPPPPPSPPA ASTPTAAARR STTSHGKDTM AKNARSLSPR HLSRRRSHVM
     FREKFYNQVI A
//