ID A0A0N1BI19_9PROT Unreviewed; 483 AA.
AC A0A0N1BI19;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=IP88_05955 {ECO:0000313|EMBL:KPF77499.1};
OS alpha proteobacterium AAP81b.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1523432 {ECO:0000313|EMBL:KPF77499.1, ECO:0000313|Proteomes:UP000037971};
RN [1] {ECO:0000313|EMBL:KPF77499.1, ECO:0000313|Proteomes:UP000037971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP81b {ECO:0000313|EMBL:KPF77499.1,
RC ECO:0000313|Proteomes:UP000037971};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPF77499.1}.
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DR EMBL; LJHX01000053; KPF77499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1BI19; -.
DR STRING; 1523432.IP88_05955; -.
DR PATRIC; fig|1523432.3.peg.2418; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000037971; 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:KPF77499.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037971};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 10..327
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 361..473
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 483 AA; 50344 MW; B62A586C94AEE8C8 CRC64;
MTRHLEPRGR RVKVLATLGP ASNSEEMIAR LIAAGADAFR INMSHGTAEA RVALIAAVRA
VEKSLGRPVT ILADLQGPKL RVGRFAAGGV ELVAGAAFRL DRSGEPGDGA RVSLPHKELF
AVLRPGARLL VDDGKIVLRV EASDDDVITT RVEVGGRISD NKGVNVPDVV VPLPALTVKD
RADLALALDH GADWIALSFV QRPEDVAEAR ALIRGQAALL AKIEKPAALE RLPEILEVAD
AVMVARGDLG VELPPQQVPP AQKRIVALAR AAGKPVVVAT QMLESMIGSP SPTRAEVSDV
ATAIYDGADA VMLSAESAAG KYPVEAVAMM DAIAREVEAD PGYFGRVHFA DVAGGGSTAA
AMSAAAASIS RTIGAKAIVC FTITGSTAGR AARERAAVPV LCLTPRPSTA RRMGLVWGVH
AIVTRDVASF EEMVEKSKRM ALRAKLAGAG DPLVLIAGVP FSTPGTTNVV HVVRLTGQEL
AGR
//
