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Database: UniProt
Entry: A0A0F7KW28_9SPHN
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ID   A0A0F7KW28_9SPHN        Unreviewed;       484 AA.
AC   A0A0F7KW28;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
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=ttuE {ECO:0000313|EMBL:AKH42985.1};
GN   ORFNames=FHS61_003107 {ECO:0000313|EMBL:MBB5734058.1}, WYH_01950
GN   {ECO:0000313|EMBL:AKH42985.1};
OS   Croceibacterium atlanticum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Croceibacterium.
OX   NCBI_TaxID=1267766 {ECO:0000313|EMBL:AKH42985.1, ECO:0000313|Proteomes:UP000034392};
RN   [1] {ECO:0000313|EMBL:AKH42985.1, ECO:0000313|Proteomes:UP000034392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=26DY36 {ECO:0000313|EMBL:AKH42985.1,
RC   ECO:0000313|Proteomes:UP000034392};
RA   Wu Y.-H., Cheng H., Wu X.-W.;
RT   "The complete genome of Altererythrobacter atlanticus strain 26DY36.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MBB5734058.1, ECO:0000313|Proteomes:UP000556014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100738 {ECO:0000313|EMBL:MBB5734058.1,
RC   ECO:0000313|Proteomes:UP000556014};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (AUG-2020) 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   -!- 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; CP011452; AKH42985.1; -; Genomic_DNA.
DR   EMBL; JACIJL010000010; MBB5734058.1; -; Genomic_DNA.
DR   RefSeq; WP_046903653.1; NZ_JACIJL010000010.1.
DR   AlphaFoldDB; A0A0F7KW28; -.
DR   STRING; 1267766.WYH_01950; -.
DR   KEGG; aay:WYH_01950; -.
DR   PATRIC; fig|1267766.3.peg.1972; -.
DR   OrthoDB; 9812123at2; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000034392; Chromosome.
DR   Proteomes; UP000556014; Unassembled WGS sequence.
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; 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:SF132; PYRUVATE KINASE 1; 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.
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:AKH42985.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034392};
KW   Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:AKH42985.1}.
FT   DOMAIN          9..326
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          359..472
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   484 AA;  53002 MW;  482196D2CF548D77 CRC64;
     MAKFDPRNRK VKILATIGPA SRDPDMLRRL FRAGADAFRF NMSHGDHAFH AENFKAVRAL
     EKQFNRPIAI LCDLQGPKLR VGTFADQRAV IPHGSRFVLD RDETPGDATR VCLPHPELFD
     LMEPGQRLLI NDGKIRLRVL EAHPDRIVCK AEVGGVISDR KGVNVPDAEI PIPALTEKDK
     RDLTFAVDQG ADWIGLSFVQ RPEDLIEARR LMGDRCALCA KIEKPQAVQR LDEIIEHSDG
     IMVARGDLGV ELNPEDVPPL QKKIVNATRL KGKPVIVATQ MLESMIESPA PTRAEVSDVA
     NAVYDGVDAV MLSAETAAGE WPEESVIMMN AIASRIEQDE DYKLRVRLLD TPPDPTVADA
     LSHSCMTIAD TVQLSVIAVF TWSGGSARRV TRERPAVPVM VLTPSVAVAR RVSLLWGAHA
     VATKDIGSFE EMIGKGKRMA LRHGFGGKGC RLVVMAGVPF GVSGATNLLH VVTMEGDELQ
     KHEG
//
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