ID A0A2K8KI08_9RHOB Unreviewed; 482 AA.
AC A0A2K8KI08;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 Name=pyk {ECO:0000313|EMBL:ATX67613.1};
GN ORFNames=BG454_02015 {ECO:0000313|EMBL:ATX67613.1};
OS Rhodobaca barguzinensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobaca.
OX NCBI_TaxID=441209 {ECO:0000313|EMBL:ATX67613.1, ECO:0000313|Proteomes:UP000228948};
RN [1] {ECO:0000313|EMBL:ATX67613.1, ECO:0000313|Proteomes:UP000228948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=alga05 {ECO:0000313|Proteomes:UP000228948};
RA Kopejtka K., Tomasch J.M., Bunk B., Koblizek M.;
RT "Revised Sequence and Annotation of the Rhodobaca barguzinensis strain
RT alga05 Genome.";
RL Submitted (NOV-2017) 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 -!- 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}.
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DR EMBL; CP024899; ATX67613.1; -; Genomic_DNA.
DR RefSeq; WP_071481926.1; NZ_SODJ01000004.1.
DR AlphaFoldDB; A0A2K8KI08; -.
DR STRING; 441209.GCA_001870665_00827; -.
DR KEGG; rbg:BG454_02015; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000228948; 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; 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.
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:ATX67613.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000228948};
KW Transferase {ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 5..322
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 482 AA; 52226 MW; 7B815FAEBC78457D CRC64;
MRRHRMIKIV ATLGPASSSY EMIRALFEAG ADVFRLNMSH GSHDEIAARH AIIRQVEADL
GRPIAILADL QGPKLRVGTF AQSSVELEDG QKFRLDLNEA EGDATRVNLP HPEIFKALEP
GAELLVNDGK IRLRVNACGP DFADCTVTVG GTISNRKGVN VPEVVLPLAA LSEKDRNDLE
FVCRLGVDWL ALSFVQRASD VTEARTLTQG RAAIISKIEK PAAIKAFDEI LAVSDGIMVA
RGDLGVELPV QNVPPIQKRL VRRTRAAAKP VIVATQMLES MIESPMPTRA EVSDVATAIY
EGADAIMLSA ESAAGQFPIE AVTTMNNVAI EVESDPTYIE IIDSSRKVNH HTIADGIVAA
ARELAEKTDI AAICCFTESG TTANLVARER PHVPIIAITP IQPVARRLAL IWGVHCETIT
GDVERFKKAV INAVRVARKY EFATEKDQIL VTAGIPFNQP GTTNILRVAP CAEHLIMTGE
PE
//
