ID W5IYI0_PSEUO Unreviewed; 476 AA.
AC W5IYI0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=PM1_0220055 {ECO:0000313|EMBL:ETM68480.1};
OS Pseudomonas sp. (strain M1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=95619 {ECO:0000313|EMBL:ETM68480.1};
RN [1] {ECO:0000313|EMBL:ETM68480.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1 {ECO:0000313|EMBL:ETM68480.1};
RX PubMed=10388678;
RA Iurescia S., Marconi A.M., Tofani D., Gambacorta A., Paterno A.,
RA Devirgiliis C., van der Werf M.J., Zennaro E.;
RT "Identification and sequencing of beta-myrcene catabolism genes from
RT Pseudomonas sp. strain M1.";
RL Appl. Environ. Microbiol. 65:2871-2876(1999).
RN [2] {ECO:0000313|EMBL:ETM68480.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M1 {ECO:0000313|EMBL:ETM68480.1};
RA Soares-Castro P.M., Santos P.M.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ETM68480.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1 {ECO:0000313|EMBL:ETM68480.1};
RX PubMed=23405299;
RA Soares-Castro P., Santos P.M.;
RT "Towards the Description of the Genome Catalogue of Pseudomonas sp. Strain
RT M1.";
RL Genome Announc. 1:E00146-E00112(2013).
RN [4] {ECO:0000313|EMBL:ETM68480.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M1 {ECO:0000313|EMBL:ETM68480.1};
RA Soares-Castro P., Santos P.M.;
RT "Decyphering the genome repertoire of Pseudomonas sp. M1 towards myrcene
RT biotransformation.";
RL Submitted (DEC-2013) 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}.
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:ETM68480.1}.
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DR EMBL; ANIR02000002; ETM68480.1; -; Genomic_DNA.
DR RefSeq; WP_009616970.1; NZ_CP094343.1.
DR AlphaFoldDB; W5IYI0; -.
DR eggNOG; COG0469; Bacteria.
DR UniPathway; UPA00109; UER00188.
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: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.
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:ETM68480.1};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 5..322
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 355..467
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 476 AA; 51767 MW; DBB36502F30F8855 CRC64;
MNSDKKVKIL ATLGPAIKGR EDIRALVDAG ANLFRLNFSH GEYADHSQRY QWVREVEAEL
GTPIGILMDL QGPKLRVGRF ENGAVMLHKG QSFTLDLMDA AGDERRVTLP HPEIIQALEP
GMSLLLDDGR IRLQVLNNHG DAIETRVLNS GELSDRKGVN VPEAVLKLSP LTAKDRRDLE
FGLELGVDWV ALSFVQRPED IEEARALIGD KAFIMAKIEK PSAVQCIEEI ARLADAIMVA
RGDLGVEVPA QNVPGIQKRI IQVCRQLGRP VVVATQMLES MRFSPAPTRA EVTDVATAVS
EGADCVMLSA ETASGQYPVE AVEMMAKIIR QVEAEPDYQG QLELNRPEPD ATASDAISCA
IRRISRILPV AVLVNYTESG SSTLRASRER PKAPILSLTP NLKAARRLSV AWGVYSVVNE
QLAHVDEICT TALEIALAQR MAQRGDTVVV TAGLPFGQPG STNMLRIETV APALSA
//
