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Database: UniProt
Entry: A0A443IIK0_9GAMM
LinkDB: A0A443IIK0_9GAMM
Original site: A0A443IIK0_9GAMM 
ID   A0A443IIK0_9GAMM        Unreviewed;       480 AA.
AC   A0A443IIK0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=ED28_02275 {ECO:0000313|EMBL:RWR03836.1};
OS   [Pantoea] beijingensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=1324864 {ECO:0000313|EMBL:RWR03836.1, ECO:0000313|Proteomes:UP000288794};
RN   [1] {ECO:0000313|EMBL:RWR03836.1, ECO:0000313|Proteomes:UP000288794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 27579 {ECO:0000313|EMBL:RWR03836.1,
RC   ECO:0000313|Proteomes:UP000288794};
RA   Xu F., Liu Y., Wang S., Yin Y., Ma Y., Zhao S., Rong C.;
RT   "Draft genome sequence of Pantoea beijingensis strain LMG 27579, an
RT   emerging pathogen to Pleurotus eryngii with potential industrial
RT   application.";
RL   Submitted (APR-2014) 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:RWR03836.1}.
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DR   EMBL; JMEE01000001; RWR03836.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A443IIK0; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000288794; 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; 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:RWR03836.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288794};
KW   Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:RWR03836.1}.
FT   DOMAIN          6..331
FT                   /note="Pyruvate kinase barrel"
FT                   /evidence="ECO:0000259|Pfam:PF00224"
FT   DOMAIN          363..477
FT                   /note="Pyruvate kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02887"
SQ   SEQUENCE   480 AA;  51594 MW;  13F97FF82E8D648C CRC64;
     MSRRLRRTKI VTTLGPATDR DNNLEKIIAA GANVVRLNFS HGTPEDHQLR ANKVREISAK
     LGRHVAILGD LQGPKIRVST FKEGKVFLSQ GDRFLLDASL GKGEGDKEKV GIDYKGLPQD
     VVPGDILLLD DGRVQLKVLD VQDLKVFTEV TVGGPLSNNK GINKLGGGLS AEALTEKDKA
     DIITAARIDV DYLAVSFPRC GEDLNYARRL AREAGCNAQI VSKVERAEAV ASQEAMDDII
     LASDVVMVAR GDLGVEIGDP ELVGIQKALI RRARQLNRAV ITATQMMESM ITNPMPTRAE
     VMDVANAVLD GTDAVMLSAE TAAGQYPAET VSAMAKVCLG AEKIPSINVS KHRLDVQFDN
     IEEAIAMSAM YAANHLQGVT AIITMTESGR TALMTSRITS GLPIFAMSRI EHTLNLTALY
     RGVTPVYFDS NNDGVAAAHD AVNLLRDKGF LMSGDLVVVT QGDVMSTSGT TNTSRVLRVE
//
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