ID H8XS20_FLAIG Unreviewed; 476 AA.
AC H8XS20;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
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 Name=pykA {ECO:0000313|EMBL:CCG54604.1};
GN OrderedLocusNames=KQS_13535 {ECO:0000313|EMBL:CCG54604.1};
OS Flavobacterium indicum (strain DSM 17447 / CIP 109464 / GPTSA100-9).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1094466 {ECO:0000313|EMBL:CCG54604.1, ECO:0000313|Proteomes:UP000007599};
RN [1] {ECO:0000313|EMBL:CCG54604.1, ECO:0000313|Proteomes:UP000007599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17447 / CIP 109464 / GPTSA100-9
RC {ECO:0000313|Proteomes:UP000007599};
RX PubMed=22582381; DOI=10.1128/JB.00420-12;
RA Barbier P., Houel A., Loux V., Poulain J., Bernardet J.F., Touchon M.,
RA Duchaud E.;
RT "Complete Genome Sequence of Flavobacterium indicum GPSTA100-9T, Isolated
RT from Warm Spring Water.";
RL J. Bacteriol. 194:3024-3025(2012).
RN [2] {ECO:0000313|Proteomes:UP000007599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17447 / CIP 109464 / GPTSA100-9
RC {ECO:0000313|Proteomes:UP000007599};
RA Barbier P., Houel A., Loux V., Poulain J., Bernardet J.-F., Touchon M.,
RA Duchaud E.;
RT "Complete genome sequence of Flavobacterium indicum GPTSA100-9T, isolated
RT from warm spring water.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; HE774682; CCG54604.1; -; Genomic_DNA.
DR RefSeq; WP_014389721.1; NC_017025.1.
DR AlphaFoldDB; H8XS20; -.
DR STRING; 1094466.KQS_13535; -.
DR KEGG; fin:KQS_13535; -.
DR PATRIC; fig|1094466.5.peg.2652; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_0_2_10; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000007599; 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: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, ECO:0000313|EMBL:CCG54604.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007599};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:CCG54604.1}.
FT DOMAIN 5..326
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 361..472
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 476 AA; 52651 MW; DB128FE2432519C9 CRC64;
MHTSKKTKIV ATLGPACSTK EVMKNMIDAG VNVFRINFSH ADYTDVKEKI DIIRELNKEF
GYTTSILADL QGPKLRVGVM KEDVIVSKGD IITFTTAEDI LGTAERVYMN YKEFPSDVNP
GERILLDDGK LIFKVIETDK KTEVKAEVVQ GGPLKSKKGV NLPNTKVSLP ALTQKDIKDA
VFAIENEVDW IALSFVRTPE DLQDLKDLIA QHSSHKIPIV AKIEKPEAVE NIDKIVINCD
GLMVARGDLG VEVPAQEVPL IQKKLILKAK TARIPVIVAT QMMETMITSL TPTRAEVNDV
ANSVMDGADA VMLSGETSVG NYPVQVIETM TSIIESVEDS SLIQVPHIAP NIRNNRFITK
SVCFHAALMA DDINAKAITT LTNSGYTAFQ ISAWRPKSHI LVFTSNKRIL TQLNLLWGVR
AFYYDKFVST DDTIEDINAI CKERKYVKKG DMVINLAAMP IANKGMVNTL RVSEVE
//
