ID A0A411HNB3_9GAMM Unreviewed; 488 AA.
AC A0A411HNB3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=pyk {ECO:0000313|EMBL:QBB71975.1};
GN ORFNames=ELE36_17285 {ECO:0000313|EMBL:QBB71975.1};
OS Pseudolysobacter antarcticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudolysobacter.
OX NCBI_TaxID=2511995 {ECO:0000313|EMBL:QBB71975.1, ECO:0000313|Proteomes:UP000291562};
RN [1] {ECO:0000313|EMBL:QBB71975.1, ECO:0000313|Proteomes:UP000291562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AQ6-296 {ECO:0000313|EMBL:QBB71975.1,
RC ECO:0000313|Proteomes:UP000291562};
RA Wei Z., Peng F.;
RT "Pseudolysobacter antarctica gen. nov., sp. nov., isolated from Fildes
RT Peninsula, Antarctica.";
RL Submitted (JAN-2019) 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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; CP035704; QBB71975.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411HNB3; -.
DR KEGG; xbc:ELE36_17285; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000291562; 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; PYRUVATE KINASE; 1.
DR PANTHER; PTHR11817:SF125; PYRUVATE KINASE II; 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:QBB71975.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000291562};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:QBB71975.1}.
FT DOMAIN 6..328
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 360..473
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 488 AA; 52396 MW; F749B1DA6C855B6B CRC64;
MLTPSRRTKI IATLGPATDA PGMLRKILEE GVDVVRLNLS HGRAEDHIER ARLVREMAME
LGREVAILAD LQGPKIRIEK FASGPVFLEP EQPFVLDCRA DADAGTIAGI GVSYLGLPRD
VKPGDTLLLD DGLIALMVLR IDGTLIHTSV IHGGWLSDRK GINRMGGGLS VDALTDKDRS
DIKLAAQMGA DFLAVSFARS AADMNQARTL LRQAGGDAAL VAKIERAEAI DVLGEIIDAS
DVVMVARGDL GVEIGDAELP GLQKKIIRET LARNKIVITA TQMMQSMVES PIPTRAEVLD
VANAVIDGTD AVMLSQESAA GKHPDKAVAA MRRVCLGAER QFESRDEFAP SSHRLDRSDQ
AIAMSAMFLS SQIGVRAIVA LTESGGTAQW LSRYRSAVPI FALSRNGAAR RRMLMYRDVY
PIDFDPQELE PTSAVHEAIL HLFTLGRLAE NDRVIVTLGD HTGRGGGTNT LKLLKVGPNG
AAEGLGDL
//
