ID A0A165CUJ3_9APHY Unreviewed; 416 AA.
AC A0A165CUJ3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Phosphoglycerate kinase {ECO:0000256|ARBA:ARBA00016471, ECO:0000256|RuleBase:RU000532};
DE EC=2.7.2.3 {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
GN ORFNames=LAESUDRAFT_369992 {ECO:0000313|EMBL:KZT03456.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT03456.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT03456.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT03456.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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|ARBA:ARBA00000642,
CC 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 EMBL; KV427644; KZT03456.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165CUJ3; -.
DR STRING; 1314785.A0A165CUJ3; -.
DR InParanoid; A0A165CUJ3; -.
DR OrthoDB; 5477183at2759; -.
DR Proteomes; UP000076871; Unassembled WGS sequence.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 3.
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; PHOSPHOGLYCERATE KINASE; 1.
DR PANTHER; PTHR11406:SF0; PHOSPHOGLYCERATE KINASE; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000724-
KW 2}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000532};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532}.
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 63..66
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 372..375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
SQ SEQUENCE 416 AA; 44354 MW; 390A6AFE88CC0994 CRC64;
MSISNKLSIT DLDLKGKRVL IRVDFNVPMQ DGKVTNPARI VAALPTIKYA LDNGASKVIL
MSHLGRPNGQ VIAKYSLEPV SKELEKQIGK PVIFVHESVG PAVEKAVNDA APGSIILLEN
LRFHIEEEGS AKDKEGKKTK AAPAKVNEFR EGLTRLGDVY VNDAFGTAHR PHSSMVGVKL
SQRAAGFLMK KELDYFAKAL EHPERPFLAI LGGAKVSDKI QLIENMLDKV DSLIICGGMA
FTFKKKLEKV SIGNSLFDEA GAEKVAALIE KAKTRKVKVV LPVDYITGDK FDKDAKTGVA
DDASGIPDGW IGLDAGPNSR ALFRTTVLEA KTILWNGPPG VFEFPAFAEG SKALLDATIE
AAQKGATVIV GGGDTATVVA QYGAEDKISH VSTGGGASLE LLEGKTLPGV AELSEK
//
