ID A0A0H4VV29_9SPHN Unreviewed; 494 AA.
AC A0A0H4VV29;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-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 ORFNames=CP97_00850 {ECO:0000313|EMBL:AKQ40908.1};
OS Aurantiacibacter atlanticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=1648404 {ECO:0000313|EMBL:AKQ40908.1, ECO:0000313|Proteomes:UP000059113};
RN [1] {ECO:0000313|EMBL:AKQ40908.1, ECO:0000313|Proteomes:UP000059113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=s21-N3 {ECO:0000313|Proteomes:UP000059113};
RX PubMed=26220886; DOI=10.1099/ijsem.0.000481;
RA Zhuang L., Liu Y., Wang L., Wang W., Shao Z.;
RT "Erythrobacter atlanticus sp. nov., a bacterium from ocean sediment able to
RT degrade polycyclic aromatic hydrocarbons.";
RL Int. J. Syst. Evol. Microbiol. 65:3714-3719(2015).
RN [2] {ECO:0000313|Proteomes:UP000059113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=s21-N3 {ECO:0000313|Proteomes:UP000059113};
RA Zhuang L., Liu Y., Shao Z.;
RT "The complete genome sequence of Erythrobacter sp. s21-N3.";
RL Submitted (APR-2015) 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; CP011310; AKQ40908.1; -; Genomic_DNA.
DR RefSeq; WP_048884387.1; NZ_CP011310.1.
DR AlphaFoldDB; A0A0H4VV29; -.
DR STRING; 1648404.CP97_00850; -.
DR KEGG; ery:CP97_00850; -.
DR PATRIC; fig|1648404.4.peg.182; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000059113; 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; 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:AKQ40908.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000059113};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 14..336
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 369..482
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 494 AA; 53278 MW; C843AA7AFEA7C201 CRC64;
MEQQQNPRLD PRGRKVKILA TTGPATANPD VLRNLFLAGA DAFRVNMSHG EHEVHAQTIA
NIRALEREFR RPIAILADLQ GPKLRVGKFA DGRATIAHGA SFTFDRSTEP GNAARVELPH
AEIFNVIEEG QRLLVNDGKI RLRVKSISAD AIVCKAEVGG VISDRKGVNV PDTEIPIPAL
TDKDRRDLAF AMEQGADWIG LSFVQRPDDL AEARKLMIGA DGKPRGALCA KIEKPQAIHR
LHEIIDLADG IMVARGDLGV ELNPEEVPPL QKKIVNATRL TGKPVIVATQ MLESMIESPA
PTRAEVSDVA NAVYDGADAV MLSAETAAGD WPEEAVLMMA NIAKQVEQDE SYLPRVRMLD
TPPDATTADA LAHACMTIAD TVKINAITVF TSSGSSARRV ARERPAVPVM VLTPSDEVGR
RVALLWGTHP VITRDIGSFE EMIAKGKRMA LRHGFGGSGS RLAVMAGVPF GQSGATNLVH
VVSVQGDELK NYES
//
