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Database: UniProt
Entry: Q2Y8W1_NITMU
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ID   Q2Y8W1_NITMU            Unreviewed;       368 AA.
AC   Q2Y8W1;
DT   20-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Pyruvate kinase {ECO:0000256|RuleBase:RU000504};
DE            EC=2.7.1.40 {ECO:0000256|RuleBase:RU000504};
GN   OrderedLocusNames=Nmul_A1507 {ECO:0000313|EMBL:ABB74810.1};
GN   ORFNames=SAMN05216403_12417 {ECO:0000313|EMBL:SEG03647.1};
OS   Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=323848 {ECO:0000313|EMBL:ABB74810.1, ECO:0000313|Proteomes:UP000002718};
RN   [1] {ECO:0000313|Proteomes:UP000002718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25196 / NCIMB 11849 / C 71
RC   {ECO:0000313|Proteomes:UP000002718};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT   25196.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABB74810.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 25196 {ECO:0000313|EMBL:ABB74810.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Richardson P.;
RT   "Complete sequence of Chromosome 1 of Nitrosospira multiformis ATCC
RT   25196.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ABB74810.1, ECO:0000313|Proteomes:UP000002718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25196 {ECO:0000313|EMBL:ABB74810.1}, and ATCC 25196 /
RC   NCIMB 11849 / C 71 {ECO:0000313|Proteomes:UP000002718};
RX   PubMed=18390676; DOI=10.1128/AEM.02722-07;
RA   Norton J.M., Klotz M.G., Stein L.Y., Arp D.J., Bottomley P.J., Chain P.S.,
RA   Hauser L.J., Land M.L., Larimer F.W., Shin M.W., Starkenburg S.R.;
RT   "Complete genome sequence of Nitrosospira multiformis, an ammonia-oxidizing
RT   bacterium from the soil environment.";
RL   Appl. Environ. Microbiol. 74:3559-3572(2008).
RN   [4] {ECO:0000313|EMBL:SEG03647.1, ECO:0000313|Proteomes:UP000236751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nl13 {ECO:0000313|EMBL:SEG03647.1,
RC   ECO:0000313|Proteomes:UP000236751};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC       {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
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DR   EMBL; CP000103; ABB74810.1; -; Genomic_DNA.
DR   EMBL; FNVK01000024; SEG03647.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2Y8W1; -.
DR   STRING; 323848.Nmul_A1507; -.
DR   KEGG; nmu:Nmul_A1507; -.
DR   eggNOG; COG0469; Bacteria.
DR   HOGENOM; CLU_015439_1_1_4; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000002718; Chromosome.
DR   Proteomes; UP000236751; 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; IPR036918; Pyrv_Knase_C_sf.
DR   InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR   NCBIfam; TIGR01064; pyruv_kin; 1.
DR   PANTHER; PTHR11817:SF3; AT14039P-RELATED; 1.
DR   PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR   Pfam; PF00224; PK; 1.
DR   PRINTS; PR01050; PYRUVTKNASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF50800; PK beta-barrel 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:ABB74810.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002718};
KW   Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:ABB74810.1}.
FT   DOMAIN          5..338
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
SQ   SEQUENCE   368 AA;  39142 MW;  5B044B11D6AEE237 CRC64;
     MTPWHRAKIV CTLGPATDAP GVIEGLISGG MDVARVNASH SDSITHSRRI EQVRRAASEA
     GQPVAILVDL PGPKFRLGNL ADDCCRLAEG AVVTLVEEGR ALEAVTDDMD GIRLPVRNPE
     LLQALRAGER VFLADGSVEL CVESSATAQS GFNAPRVRCE VLIGGVVRSG SGINVPESAL
     LELVPTDDDR QHLAFALARQ VEWIGISFVQ SVDEIHRVRA LLPSTGAPLV MAKIEKRKAL
     VNLEEIVEAA DGVMVARGDL GVETDLAEIA LIQKRIISVA NARARPVITA TQMLESMVAY
     EHPTRAEVTD VANAVLDGTD AVMLSAETAI GQFPVTAVKI LQRVIAATEA RHNGSPNSKM
     RAGMTGVR
//
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