ID A9TZX1_PHYPA Unreviewed; 520 AA.
AC A9TZX1;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 106.
DE RecName: Full=Pyruvate kinase {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
GN ORFNames=PHYPA_021797 {ECO:0000313|EMBL:PNR35947.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR35947.1};
RN [1] {ECO:0000313|EMBL:PNR35947.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c17_8050V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR35947.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c17_8050V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c17_8050V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC EC=2.7.1.40; Evidence={ECO:0000256|ARBA:ARBA00001174,
CC ECO:0000256|RuleBase:RU000504};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5. {ECO:0000256|ARBA:ARBA00004997,
CC ECO:0000256|RuleBase:RU000504}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
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DR EMBL; ABEU02000017; PNR35947.1; -; Genomic_DNA.
DR RefSeq; XP_001784162.1; XM_001784110.1.
DR AlphaFoldDB; A9TZX1; -.
DR STRING; 3218.A9TZX1; -.
DR PaxDb; 3218-PP1S392_18V6-4; -.
DR EnsemblPlants; Pp3c17_8050V3.1; Pp3c17_8050V3.1; Pp3c17_8050.
DR EnsemblPlants; Pp3c17_8050V3.10; Pp3c17_8050V3.10; Pp3c17_8050.
DR EnsemblPlants; Pp3c17_8050V3.11; Pp3c17_8050V3.11; Pp3c17_8050.
DR EnsemblPlants; Pp3c17_8050V3.2; Pp3c17_8050V3.2; Pp3c17_8050.
DR EnsemblPlants; Pp3c17_8050V3.3; Pp3c17_8050V3.3; Pp3c17_8050.
DR EnsemblPlants; Pp3c17_8050V3.4; Pp3c17_8050V3.4; Pp3c17_8050.
DR EnsemblPlants; Pp3c17_8050V3.5; Pp3c17_8050V3.5; Pp3c17_8050.
DR EnsemblPlants; Pp3c17_8050V3.9; Pp3c17_8050V3.9; Pp3c17_8050.
DR Gramene; Pp3c17_8050V3.1; Pp3c17_8050V3.1; Pp3c17_8050.
DR Gramene; Pp3c17_8050V3.10; Pp3c17_8050V3.10; Pp3c17_8050.
DR Gramene; Pp3c17_8050V3.11; Pp3c17_8050V3.11; Pp3c17_8050.
DR Gramene; Pp3c17_8050V3.2; Pp3c17_8050V3.2; Pp3c17_8050.
DR Gramene; Pp3c17_8050V3.3; Pp3c17_8050V3.3; Pp3c17_8050.
DR Gramene; Pp3c17_8050V3.4; Pp3c17_8050V3.4; Pp3c17_8050.
DR Gramene; Pp3c17_8050V3.5; Pp3c17_8050V3.5; Pp3c17_8050.
DR Gramene; Pp3c17_8050V3.9; Pp3c17_8050V3.9; Pp3c17_8050.
DR eggNOG; KOG2323; Eukaryota.
DR HOGENOM; CLU_015439_0_1_1; -.
DR InParanoid; A9TZX1; -.
DR OMA; AMSKPHR; -.
DR OrthoDB; 5483908at2759; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000006727; Chromosome 17.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR GO; GO:0004743; F:pyruvate kinase activity; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 2.40.33.10; PK beta-barrel domain-like; 1.
DR Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 1.
DR InterPro; IPR001697; Pyr_Knase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR InterPro; IPR018209; Pyrv_Knase_AS.
DR InterPro; IPR015793; Pyrv_Knase_brl.
DR InterPro; IPR015795; Pyrv_Knase_C.
DR InterPro; IPR036918; Pyrv_Knase_C_sf.
DR InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR NCBIfam; TIGR01064; pyruv_kin; 1.
DR PANTHER; PTHR11817:SF3; AT14039P-RELATED; 1.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF52935; PK C-terminal domain-like; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000504};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000504};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU000504};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317};
KW Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 25..350
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 385..505
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 520 AA; 56117 MW; 391A1957E8AD8477 CRC64;
MATKTDIAHI LGLDANEDDG HLKISKTKIV CTLGPKSREV HVLEKLLRAG MNVARFNFSH
GTHEYHQYTL DSLRQAMANT QTMCAVLLDT KGPEIRTGSL AAGKPIQLKR NNEIWITTDY
SHLGDENMIA MSYAKLAVDL EPGNTILCSD GTITMTVLDC HPEKGMVKAR CENTAMLGEK
KNVNLPGIVV DLPTITQKDI DDIMQWGVPN KIDFIAASFV RKGSDVVTIK KLLGEASDSI
HVISKVENQE GLVNFDDILK ETDGVMVARG DLGMEIPTEK IFLAQKMMIY KCNSAGKPVV
TATQMLESMI KSPRPTRAEA TDVANAVLDG TDAVMLSGET ANGSYPELAV AVMSQICQEA
EAALDYASIF KEIMKSVPLP MSPLESLASS AVRTANKVRA SLIIVLTRGG STARLVAKYR
PCVPILSVAV PVMTTDGLEW TFSAPSPAHH SLCCRGLIPL LAEGSAKATD SESTEEILNA
AVKYALKRKL CLVSDSVVAL HRIGVASVIK IIEVKDLASS
//