ID Z9JXT6_9MICO Unreviewed; 490 AA.
AC Z9JXT6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Pyruvate kinase {ECO:0000256|ARBA:ARBA00018587, ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
GN ORFNames=BF93_07350 {ECO:0000313|EMBL:EWS82828.1};
OS Brachybacterium phenoliresistens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=396014 {ECO:0000313|EMBL:EWS82828.1, ECO:0000313|Proteomes:UP000023067};
RN [1] {ECO:0000313|EMBL:EWS82828.1, ECO:0000313|Proteomes:UP000023067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W13A50 {ECO:0000313|EMBL:EWS82828.1,
RC ECO:0000313|Proteomes:UP000023067};
RA Wang X.;
RT "Genome sequence of Brachybacterium phenoliresistens strain W13A50.";
RL Submitted (FEB-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 -!- 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:EWS82828.1}.
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; JDYK01000002; EWS82828.1; -; Genomic_DNA.
DR RefSeq; WP_038370280.1; NZ_KK069988.1.
DR AlphaFoldDB; Z9JXT6; -.
DR STRING; 396014.BF93_07350; -.
DR PATRIC; fig|396014.3.peg.461; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_0_2_11; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000023067; 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: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:EWS82828.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000023067};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:EWS82828.1}.
FT DOMAIN 1..322
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 353..465
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 490 AA; 53239 MW; FEBA562ED3A635E0 CRC64;
MRKAKIVCTL GPATNTYEQI RTLIESGMNV ARMNLSHGTH DDHEKVYANI RRAADDLGRN
VAVLVDLQGP KIRLGKFEDG PHQLEVGDSF VITTEDIIGT RERVSTTFKG LPGDCRPGDV
LLIDDGKVSV RVTEVTDTDV RTVVEVPGPV SDSKGINLPG VAVSVPAMSE KDIADLRWGL
RLGADLIALS FVRDAHDMDD VLRIMHEEER RVPVIAKIEK PQAVRALRQI VGAFDGIMVA
RGDLGVELPL EQVPLVQKRA IELARRNAKP VIVATQVLES MITAPRPTRA EASDCANAIL
DGADAVMLSG ETSVGAYPFE AVRTMARIIT NTEENGADRI MPLGTIPHTR GGAITRAAAE
IGDQLSAQYL VTFTESGDTA RRLARLRPTI PLLAMTPYEH VRHQLSMSWG IEAQLVPMQR
NTDEMVRVVD DLLREQKGLQ PGDLVIIAAG SPPGVHGSTN TLRVHRIGDL DGTESARIEA
DRIAQGPQDI
//