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Database: UniProt
Entry: A9TZX1_PHYPA
LinkDB: A9TZX1_PHYPA
Original site: A9TZX1_PHYPA 
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
//
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