ID A0A0X9VTR6_9GAMM Unreviewed; 470 AA.
AC A0A0X9VTR6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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:AMA64683.1};
GN ORFNames=AUT07_00090 {ECO:0000313|EMBL:AMA64683.1};
OS Candidatus Arsenophonus lipoptenae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Arsenophonus.
OX NCBI_TaxID=634113 {ECO:0000313|EMBL:AMA64683.1, ECO:0000313|Proteomes:UP000069926};
RN [1] {ECO:0000313|EMBL:AMA64683.1, ECO:0000313|Proteomes:UP000069926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB {ECO:0000313|EMBL:AMA64683.1,
RC ECO:0000313|Proteomes:UP000069926};
RA Novakova E., Hypsa V., Nguyen P., Husnik F., Darby A.C.;
RT "Genome sequence of Ca. Arsenophonus lipopteni, the exclusive symbiont of a
RT blood sucking fly Lipoptena cervi (Diptera: Hippoboscidae).";
RL Submitted (JAN-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 -!- 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP013920; AMA64683.1; -; Genomic_DNA.
DR RefSeq; WP_066282702.1; NZ_CP013920.1.
DR AlphaFoldDB; A0A0X9VTR6; -.
DR STRING; 634113.AUT07_00090; -.
DR KEGG; asy:AUT07_00090; -.
DR PATRIC; fig|634113.3.peg.88; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000069926; 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 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:AMA64683.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000069926};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:AMA64683.1}.
FT DOMAIN 1..325
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 356..468
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 470 AA; 51619 MW; 97A22FE702E64EB0 CRC64;
MKKTKIVCTI GPRTESKEIL SQLLDAGMDV MRLNFSHGNH EEHGQRIKNL RSVCIEQNKQ
AAILLDTKGP EIRTMYLKKG KEVSLITGQN FILTTDTSVI GNHDRVAVTY SGLTNDLHPG
NIILIDDGLI SMEVLFIKSN NIYCKVLNNG DLGENKGVNL PGVFISLPAL SEKDKQDLIF
GYQQGIDFIA ASFIRKRADV EEIRNHLIQH SDKNIQIISK IENQEGLNNF DEILEASDGI
MVARGDLGVE IPVEEVIFAQ KMMIEKCVAA RKIVITATQL LDSMIKNPRP TRAEAGDVAN
AILDGTDAVM LSGESAKGKY PIEAVKIMAT ICDRTDRVMA SRIDNSKINQ KLRITEAVCR
GAIEMAEKLN SKLIIVATYG GKSAKSVRKY FPTAPILALT TNEETARQLL LVKGVIPQLV
KEIASTDDFY RIGKQIALRN NMATTNDVVV MVSGALVSTG TTNTSSVHIL
//
