ID Q4QL04_HAEI8 Unreviewed; 478 AA.
AC Q4QL04;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 104.
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=pykA {ECO:0000313|EMBL:AAX88293.1};
GN OrderedLocusNames=NTHI1479 {ECO:0000313|EMBL:AAX88293.1};
OS Haemophilus influenzae (strain 86-028NP).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=281310 {ECO:0000313|EMBL:AAX88293.1, ECO:0000313|Proteomes:UP000002525};
RN [1] {ECO:0000313|EMBL:AAX88293.1, ECO:0000313|Proteomes:UP000002525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=86-028NP {ECO:0000313|EMBL:AAX88293.1,
RC ECO:0000313|Proteomes:UP000002525};
RX PubMed=15968074; DOI=10.1128/JB.187.13.4627-4636.2005;
RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA Munson R.S.Jr.;
RT "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL J. Bacteriol. 187:4627-4636(2005).
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; CP000057; AAX88293.1; -; Genomic_DNA.
DR RefSeq; WP_005687732.1; NC_007146.2.
DR AlphaFoldDB; Q4QL04; -.
DR KEGG; hit:NTHI1479; -.
DR HOGENOM; CLU_015439_8_0_6; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000002525; 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 CDD; cd00288; Pyruvate_Kinase; 1.
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:AAX88293.1};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:AAX88293.1}.
FT DOMAIN 6..331
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 363..473
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 478 AA; 51085 MW; BA946BD3F58F7126 CRC64;
MSRRLRRTKI VCTMGPSTDR DNNLEKIIAA GANVVRMNFS HGTPDDHIGR AERVRSIAKK
LGKTVAILGD LQGPKIRVST FKDGKIFLNV GDKFILDAEL PKGEGTQESV GLDYKTLPQD
VVPGDILLLD DGRVQLKVLS TDGAKVFTEV TVGGPLSNNK GINKLGGGLS ADALTEKDKA
DIITAARIGV DFLAVSFPRS SADLNYAREL AQQAGLNAKI VAKVERAETV ANDEAMDDII
LASDVIMVAR GDLGVEIGDP ELVGVQKKLI RRSRQLNRAV ITATQMMESM ISNPMPTRAE
VMDVANAVLD GTDAVMLSAE TAAGQYPSET VAAMASVCLG AEKMPSINVS RHRMDKEFET
IEESVAMSAM YAANHMKGVA AIVTLTSTGR TPLLMSRISS GLPIFALSRN QETLNLCALY
RGVTPIYHGE ESRTEAGAKA ALQSLKEKGY LSTGDLVLVT QGGQGATQTN VCRTLIVE
//
