ID A0A0A7FUM6_9CLOT Unreviewed; 475 AA.
AC A0A0A7FUM6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, 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 Name=pyk {ECO:0000313|EMBL:AIY83287.1};
GN ORFNames=U729_761 {ECO:0000313|EMBL:AIY83287.1};
OS Clostridium baratii str. Sullivan.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1415775 {ECO:0000313|EMBL:AIY83287.1, ECO:0000313|Proteomes:UP000030635};
RN [1] {ECO:0000313|EMBL:AIY83287.1, ECO:0000313|Proteomes:UP000030635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sullivan {ECO:0000313|EMBL:AIY83287.1};
RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA Karavis M.A., Smith L.A.;
RT "Genomic sequences of six botulinum neurotoxin-producing strains
RT representing three clostridial species illustrate the mobility and
RT diversity of botulinum neurotoxin genes.";
RL Infect. Genet. Evol. 30:102-113(2014).
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}.
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DR EMBL; CP006905; AIY83287.1; -; Genomic_DNA.
DR RefSeq; WP_039311778.1; NZ_CP006905.1.
DR AlphaFoldDB; A0A0A7FUM6; -.
DR STRING; 1561.NPD11_2244; -.
DR KEGG; cbv:U729_761; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_0_2_9; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000030635; 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: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.
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:AIY83287.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030635};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:AIY83287.1}.
FT DOMAIN 1..327
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 361..471
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 475 AA; 50580 MW; 7B524105453B8AB1 CRC64;
MKKTKMICTI GPASENEEIL SKIIEAGMNA SRHNFSHGDH EEHKGRILKV KELAKKYNKE
IAVVLDTKGP EIRTGKFEPS KIELQKGSEF TIYVGPEAQD LVGDATKCSV TYDGLANDVK
PGNTILIDDG LVGLEVKAVE GNAVKCEVKN TGLVGTHKGV NVPGVSIQLP ALTKKDESDL
IFGCEIGVNM IAASFVRKAK DVQAIRKVLD DNGGKDILIC SKIENQEGVD NIDSILEESD
AIMVARGDLG VEIPIENVPA VQKMIIEKCN KAGKPVVTAT QMLDSMIRNP RPTRAEVSDV
ANAILDGTDA IMLSGESANG SYPVEAVQTM AKIARETEKQ LSYKVAVSQA TNHVPAIAGV
ISRAACNAAN ELQASAIVSS TQSGATAKRL SQCRPECPII AVTPSETVAK QLAFSWGVYP
IVADKVESTD EMMNKSVETA KNNGFVNEGD TVVIAAGVPV DEIGATNLMK VTVVK
//
