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Database: UniProt
Entry: A0A291P2N6_9GAMM
LinkDB: A0A291P2N6_9GAMM
Original site: A0A291P2N6_9GAMM 
ID   A0A291P2N6_9GAMM        Unreviewed;       488 AA.
AC   A0A291P2N6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=BEI_0156 {ECO:0000313|EMBL:ATJ81143.1};
OS   Halomonas beimenensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=475662 {ECO:0000313|EMBL:ATJ81143.1, ECO:0000313|Proteomes:UP000219993};
RN   [1] {ECO:0000313|EMBL:ATJ81143.1, ECO:0000313|Proteomes:UP000219993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NTU-111 {ECO:0000313|EMBL:ATJ81143.1,
RC   ECO:0000313|Proteomes:UP000219993};
RX   PubMed=29026163;
RA   Chen Y.H., Lin S.S., Shyu Y.T.;
RT   "Revealing the Saline Adaptation Strategies of the Halophilic Bacterium
RT   Halomonas beimenensis through High-throughput Omics and Transposon
RT   Mutagenesis Approaches.";
RL   Sci. Rep. 7:13037-13037(2017).
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   -!- 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; CP021435; ATJ81143.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A291P2N6; -.
DR   KEGG; hbe:BEI_0156; -.
DR   OrthoDB; 9812123at2; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000219993; Chromosome.
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; 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; PYRUVATE KINASE; 1.
DR   PANTHER; PTHR11817:SF125; PYRUVATE KINASE II; 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, ECO:0000313|EMBL:ATJ81143.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219993};
KW   Transferase {ECO:0000256|RuleBase:RU000504}.
FT   DOMAIN          9..334
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          366..481
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   488 AA;  51752 MW;  58204E862321DE71 CRC64;
     MPHHPAPVRR TKIVATLGPA SDREGVLERM IAAGVDVVRL NFSHGSADDH RRRLAAVREI
     ADRLGRSVAA LGDLQGPKIR IARFSDGKVS LAEGAPFVID VALDAEAGDA ERVGCDYKAL
     ASDVAAGDRL LLDDGRVVLD VARVEGSAIH TTVVVGGELS NNKGINKQGG GLSAPALTDK
     DRADLETAVA IGVDYLAVSF PRSAADMHEA RELLGDAGKE IGLVAKLERA EAVASDATLD
     AIIEASEAVM VARGDLGVEI GDEKLIGTQK RIIKHARSHN RAVITATQMM ESMIEAPLPT
     RAEVFDVANA VLDATDAVML SAETAAGDFP VETVEAMARV CLGAERERIA QESSHRIHEG
     FERIDETIAL SAMYAANHLT GVAAIACMTA TGYTPLIASR IRSRLPIVGL AHNPVAQRRM
     ALYRGVISLP FDTSDMTAAE LNDRALERVV TQGIAVPGDH VILTRGDHMN AHGGTNTLRI
     LAVETHHE
//
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