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Database: UniProt
Entry: A0A2K3P7N2_TRIPR
LinkDB: A0A2K3P7N2_TRIPR
Original site: A0A2K3P7N2_TRIPR 
ID   A0A2K3P7N2_TRIPR        Unreviewed;       748 AA.
AC   A0A2K3P7N2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
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};
DE   Flags: Fragment;
GN   ORFNames=L195_g007896 {ECO:0000313|EMBL:PNY11292.1};
OS   Trifolium pratense (Red clover).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium.
OX   NCBI_TaxID=57577 {ECO:0000313|EMBL:PNY11292.1, ECO:0000313|Proteomes:UP000236291};
RN   [1] {ECO:0000313|EMBL:PNY11292.1, ECO:0000313|Proteomes:UP000236291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:PNY11292.1};
RX   PubMed=24500806; DOI=10.3732/ajb.1300340;
RA   Istvanek J., Jaros M., Krenek A., Repkova J.;
RT   "Genome assembly and annotation for red clover (Trifolium pratense;
RT   Fabaceae).";
RL   Am. J. Bot. 101:327-337(2014).
RN   [2] {ECO:0000313|EMBL:PNY11292.1, ECO:0000313|Proteomes:UP000236291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:PNY11292.1};
RX   PubMed=28382043; DOI=10.3389/fpls.2017.00367;
RA   Istvanek J., Dluhosova J., Dluhos P., Patkova L., Nedelnik J., Repkova J.;
RT   "Gene Classification and Mining of Molecular Markers Useful in Red Clover
RT   (Trifolium pratense) Breeding.";
RL   Front. Plant Sci. 8:367-367(2017).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PNY11292.1}.
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DR   EMBL; ASHM01004439; PNY11292.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K3P7N2; -.
DR   STRING; 57577.A0A2K3P7N2; -.
DR   Proteomes; UP000236291; Unassembled WGS sequence.
DR   ExpressionAtlas; A0A2K3P7N2; baseline.
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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 3.
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; 2.
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:UP000236291};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..748
FT                   /note="Phosphoglycerate kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014396017"
FT   NON_TER         748
FT                   /evidence="ECO:0000313|EMBL:PNY11292.1"
SQ   SEQUENCE   748 AA;  84566 MW;  150B0ED6DD65630E CRC64;
     MQTVSAALVI ALFNLVNLMA QLMNILHEPV FLNISCFYDF PKLLKHKTCS YVPKLAKFHK
     SNGALLAMQG NVELAGPVVN LFNHKIYINN GEELNGIPHI QTLREFPREE LFGKVVMVRF
     ESNILLKQEY NEKNQSDFNA LFTIKYLHEA GANVILVGDW KTNTSELHTA TVAGILQRQV
     VPLQGISCNK LSEINGFKKE NIYLLENLNN IKDEVANCLK FARVLSSGVD IFVNDSFSNS
     HKVLASTVGV TRFCYARIAG FHFEEKLRFV KNLAEANKKP YVAIIGGGNL AMKAASFRFL
     ASRCQCFIFV GMMSFQIMNA LGVPVPIDLV DRKAFSEALD IVRRARDNNV QILYPKDFWC
     RNKNDPKQLH VFPSHGLLDG WVPIDLGPVS LDEIGNLLRW TYHTCNTAPY MLMLLEFVHV
     VNVMTKCYLV VAIAVLYHCS EAKFEQHAIF REPQFSTLKI IWIGPVKFAN RSEHTNGASK
     LAKILVQLSQ GNCETTIVGT TACNLVRQET SSLSSINMVE NASVVWEFLK GRKLPGVMAV
     DRAYPFEINW NNIYSVPTQS LVVDIGSGNG LFLLEMAKRR KDLNFLGLEM NEKLVLRCLD
     SIQEFGIKNG HFIATNATST FRSIVSSYQG ELVLVSIQCP NPDFNKPEHR WRMLQRSLIE
     AVVDLLASGG KVFLQSDVKE VAQKMKEQFM RYGKGKLVLE HGQSDWLDEN PLGVRSDWEK
     HVLERRAPMY RMMFSKSSEK SEVLISNE
//
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