ID A0A2K8UI82_9GAMM Unreviewed; 619 AA.
AC A0A2K8UI82;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=pyruvate kinase {ECO:0000256|ARBA:ARBA00012142};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142};
GN ORFNames=THSYN_30740 {ECO:0000313|EMBL:AUB85284.1};
OS Candidatus Thiodictyon syntrophicum.
OG Plasmid pts417 {ECO:0000313|Proteomes:UP000232638}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiodictyon.
OX NCBI_TaxID=1166950 {ECO:0000313|EMBL:AUB85284.1, ECO:0000313|Proteomes:UP000232638};
RN [1] {ECO:0000313|EMBL:AUB85284.1, ECO:0000313|Proteomes:UP000232638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cad16T {ECO:0000313|EMBL:AUB85284.1,
RC ECO:0000313|Proteomes:UP000232638};
RC PLASMID=Plasmid pts417 {ECO:0000313|Proteomes:UP000232638};
RA Luedin S.M., Pothier J.F., Danza F., Storelli N., Wittwer M., Tonolla M.;
RT "Complete genome sequence of Candidatus 'Thiodictyon syntrophicum' sp. nov.
RT strain Cad16T, a photolithoautotroph purple sulfur bacterium isolated from
RT an alpine meromictic lake.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5. {ECO:0000256|ARBA:ARBA00004997}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663}.
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DR EMBL; CP020371; AUB85284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K8UI82; -.
DR KEGG; tsy:THSYN_30740; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000232638; Plasmid pts417.
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; 2.
DR Gene3D; 2.40.33.10; PK beta-barrel domain-like; 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; IPR015806; Pyrv_Knase_insert_dom_sf.
DR PANTHER; PTHR11817:SF76; PLASTIDIAL PYRUVATE KINASE 4, CHLOROPLASTIC; 1.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR Pfam; PF00224; PK; 2.
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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AUB85284.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Plasmid {ECO:0000313|EMBL:AUB85284.1};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:AUB85284.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000232638};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AUB85284.1}.
FT DOMAIN 137..213
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 364..578
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
SQ SEQUENCE 619 AA; 66830 MW; C8EA8462E2EAC7E7 CRC64;
MPPTPAQVAA LAAQLVALRD GALALEQRFG DELAAIAPQQ RASARNLLHY LSVRRHDIRA
LQQDLSALGL SSLGVLEPHA LASLNAVIGV LAQLQDAAPG GGHPPLPPPP VDFRSGPQRL
REHALALLGP EPQGRLVRIM VTMPSEAATD AQLVQDLLDA GMDVMRINCA HDGPAEWAAM
VENLRRAEQS RGRSCRVAMD LAGPKLRTGA LRASGRVQRL APQRDCFGRL TRPGRVWLTP
AEAAEPRPPG LRLRLEISGG LLGQLAMGDQ LEFTDARGQE HRLLVREARG ASWVAEIEQT
AYVEEATRVT ARRDGETVGS GAFINVPEVI EPIALAVGEL LILTRCDAPG QGAERAADGT
VVTPAQVHCT LATAFEFARP GHTVWFDDGK IGGVVAANDG ERITVSITQT GPKGARLRAE
KGINFPDTPL AMSALTDKDL ADLPAIVRLA DMVQLSFVRE PQDLAQLHAE LDRLGAQRMG
VVLKIENRRA FENLPRLLLA SLHRPPVGVM IARGDLAVEV GFERLSEVQQ EILWLCEAAH
VPVIWATQIL EGMAKTGAPS RAEVSDAGMS IMAECAMLNK GPRIVETVRF LAGIIDRMDE
HYRKQRATLR RLAVADLED
//
