ID A0A077P2G5_XENBV Unreviewed; 469 AA.
AC A0A077P2G5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Pyruvate kinase {ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|RuleBase:RU000504};
GN Name=pykF {ECO:0000313|EMBL:CDH18620.1};
GN ORFNames=XBKQ1_140002 {ECO:0000313|EMBL:CDH18620.1};
OS Xenorhabdus bovienii str. kraussei Quebec.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1398203 {ECO:0000313|EMBL:CDH18620.1, ECO:0000313|Proteomes:UP000028500};
RN [1] {ECO:0000313|EMBL:CDH18620.1, ECO:0000313|Proteomes:UP000028500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=kraussei Quebec {ECO:0000313|Proteomes:UP000028500};
RA Murfin K., Klassen J., Lee M., Forst S., Stock P., Goodrich-Blair H.;
RT "Sub-species coevolution in mutualistic symbiosis.";
RL Submitted (JUL-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 -!- 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}.
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:CDH18620.1}.
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DR EMBL; CBSY010000046; CDH18620.1; -; Genomic_DNA.
DR RefSeq; WP_038206196.1; NZ_HG427502.1.
DR AlphaFoldDB; A0A077P2G5; -.
DR GeneID; 77310934; -.
DR HOGENOM; CLU_015439_0_0_6; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000028500; 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 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:SF3; AT14039P-RELATED; 1.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 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:CDH18620.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028500};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:CDH18620.1}.
FT DOMAIN 1..325
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 469 AA; 50410 MW; 280F5F5C3F7554CF CRC64;
MKKTKIVCTI GPKTESETKL TELLNAGMNV MRLNFSHGDY EEHGQRIKNL RAVTAKTGKK
AAILLDTKGP EIRTIKLEGG NDVSLTAGQT FTFTTDKSVI GNQECVAVTY AGLPADLKPG
NTILVDDGLI AMTVKNVTET EVICEVLNNG DLGENKGVNL PNVAINLPAL AEKDKQDLIF
GCEQGVDFVA ASFIRKRSDV LEIRDHLKAH GGEHIQIISK IENQEGLNNF DEIMEASDGI
MVARGDLGVE IPVEEVIFAQ KMMIEKCNAA RKVVITATQM LDSMIKNPRP TRAEAGDVAN
AILDGTDAVM LSGESAKGKY PIEAVSIMAT ICERTDRVMS SRIEITKAQK LRVTEAVCRG
AVEIAEKLEA PLIVVATYGG KSARSIRKYF PNAPILALTT NEITARQLLL VKGVSTQIVK
EIASTDDFYR IGKEAALASG MANKGDAVVM ISGALVPSGT TNTSSVHVL
//
