GenomeNet

Database: UniProt
Entry: A0A024FFI5_9FLAO
LinkDB: A0A024FFI5_9FLAO
Original site: A0A024FFI5_9FLAO 
ID   A0A024FFI5_9FLAO        Unreviewed;       477 AA.
AC   A0A024FFI5;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=WPG_1207 {ECO:0000313|EMBL:BAO75437.1};
OS   Winogradskyella sp. PG-2.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Winogradskyella.
OX   NCBI_TaxID=754409 {ECO:0000313|EMBL:BAO75437.1, ECO:0000313|Proteomes:UP000031636};
RN   [1] {ECO:0000313|EMBL:BAO75437.1, ECO:0000313|Proteomes:UP000031636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG-2 {ECO:0000313|EMBL:BAO75437.1,
RC   ECO:0000313|Proteomes:UP000031636};
RX   PubMed=24874677; DOI=10.1128/genomeA.00490-14;
RA   Kumagai Y., Yoshizawa S., Oshima K., Hattori M., Iwasaki W., Kogure K.;
RT   "Complete Genome Sequence of Winogradskyella sp. Strain PG-2, a
RT   Proteorhodopsin-Containing Marine Flavobacterium.";
RL   Genome Announc. 2:e00490-14(2014).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP014583; BAO75437.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024FFI5; -.
DR   STRING; 754409.WPG_1207; -.
DR   KEGG; win:WPG_1207; -.
DR   HOGENOM; CLU_015439_0_2_10; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000031636; 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:BAO75437.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031636};
KW   Transferase {ECO:0000256|RuleBase:RU000504}.
FT   DOMAIN          4..325
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          360..471
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   477 AA;  52903 MW;  420CD3624C1773FB CRC64;
     MSNKKTKIVA TLGPATSKKE VLKAMLDEGA NVFRVNFSHA DYKDVEERVK LIRELNDEFG
     YNASILGDLQ GPKLRVGMMK GEVVVNPGDE IIFATGERFE GTKERVYMTY DKFPQDAKPG
     ERILLDDGKL HFEVVSTDGK SEVKAKVIQG GPLKSKKGVN LPNTNISQPA LTEKDVEDAI
     FACKLGVDWI ALSFVRHAED LMQLEKLISE HSDHKIPIIA KIEKPEAVEN IDKIVAYCDG
     LMVARGDLGV EIPAEEVPLV QKQLVLRAKR ARIPVIIATQ MMETMITSLT PTRAEVNDVA
     NSVMDGADAV MLSGETSVGQ YPVQVIRQMA NIIRSVEDSP LIEVPQSPPH IRTKRYITKA
     ICYHAANMAN EINAKAISTL TNSGYTAFQI SAWRPQAHIL VFTSNKRILT QLNLLWGVTA
     FFYDKFVSTD ETVRDTNRIA KKSGYLDKGD MVISLASMPI AEKGMVNTLR VREISNE
//
DBGET integrated database retrieval system