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Database: UniProt
Entry: U1PNY9_9EURY
LinkDB: U1PNY9_9EURY
Original site: U1PNY9_9EURY 
ID   U1PNY9_9EURY            Unreviewed;       492 AA.
AC   U1PNY9;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
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};
DE   Flags: Fragment;
GN   ORFNames=J07HB67_01184 {ECO:0000313|EMBL:ERH12171.1};
OS   halophilic archaeon J07HB67.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales.
OX   NCBI_TaxID=1085029 {ECO:0000313|EMBL:ERH12171.1};
RN   [1] {ECO:0000313|EMBL:ERH12171.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23637883;
RA   Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., Heidelberg K.B.,
RA   Allen E.E.;
RT   "Assembly-driven community genomics of a hypersaline microbial ecosystem.";
RL   PLoS ONE 8:E61692-E61692(2013).
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|RuleBase:RU000504};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|ARBA:ARBA00001958};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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   -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC       {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
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DR   EMBL; KE356582; ERH12171.1; -; Genomic_DNA.
DR   AlphaFoldDB; U1PNY9; -.
DR   STRING; 1085029.J07HB67_01184; -.
DR   HOGENOM; CLU_015439_0_2_2; -.
DR   UniPathway; UPA00109; UER00188.
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; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   Gene3D; 3.50.30.10; Phosphohistidine domain; 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; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR001697; Pyr_Knase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
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; PF00391; PEP-utilizers; 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; SSF52009; Phosphohistidine domain; 1.
DR   SUPFAM; SSF52935; PK C-terminal domain-like; 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|RuleBase:RU000504};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:ERH12171.1};
KW   Transferase {ECO:0000256|RuleBase:RU000504}.
FT   DOMAIN          9..226
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          261..375
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
FT   DOMAIN          408..478
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ERH12171.1"
SQ   SEQUENCE   492 AA;  51523 MW;  2BF89E00FA338EC3 CRC64;
     EGETATPDRV GLSYSVAASE PGDKLLLDDG RIETTVTSVD GDTVYATVDS GGPLDSRKGV
     NLPGVDLGLT PVTAADEAEL AVAGEADVDF VAASFVRDAA DVYAVQDAME AHGAGDVPLV
     AKIERRGAVE NLDEIVEAAY GVMVARGDLG VECPLEEVPV IQKRIIRTCV ETGTPVITAT
     EMLDSMVAAR RPTRAEASDV ANAVLDGTDA VMLSGETAVG DHPARVVETM DRIVRRVEDS
     HQYAESREQR VPVADDDSRT EALARSARFL ARDTDASAVV TASESGYTAR KTAKFRPAVP
     VVATTPADEV RRQLALSWGV RPVAAGYSES VEEVMDDAVD AALSTGVADS GDTLVVLSGM
     MTELEGNSTN TLKLHVAAET VATGRNVVGG RVCAPLARVP DGDLSGVPDD DIAYLPATFD
     AEFHGDTGKL AGVVDARAGM TGYPAIVARE REIPMVSGAP VPARIDDETL VTLDAERGVV
     YEGDVLRHAR GR
//
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