BUK_CLOP1
ID BUK_CLOP1 Reviewed; 356 AA.
AC Q0TMV4; Q9ZNE5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Butyrate kinase;
DE Short=BK;
DE EC=2.7.2.7;
GN Name=buk; Synonyms=bukA; OrderedLocusNames=CPF_2656;
OS Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS 6125 / NCTC 8237 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195103;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10585557; DOI=10.1111/j.1574-6968.1999.tb08863.x;
RA Kaji M., Taniguchi Y., Matsushita O., Katayama S., Miyata S., Morita S.,
RA Okabe A.;
RT "The hydA gene encoding the H(2)-evolving hydrogenase of Clostridium
RT perfringens: molecular characterization and expression of the gene.";
RL FEMS Microbiol. Lett. 181:329-336(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A;
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
CC -!- FUNCTION: Catalyzes the conversion of butyryl-CoA through butyryl
CC phosphate to butyrate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + butanoate = ADP + butanoyl phosphate;
CC Xref=Rhea:RHEA:13585, ChEBI:CHEBI:17968, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58079, ChEBI:CHEBI:456216; EC=2.7.2.7;
CC -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000305}.
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DR EMBL; AB016775; BAA74725.1; -; Genomic_DNA.
DR EMBL; AB035092; BAA95935.1; -; Genomic_DNA.
DR EMBL; CP000246; ABG83930.1; -; Genomic_DNA.
DR RefSeq; WP_003454444.1; NC_008261.1.
DR AlphaFoldDB; Q0TMV4; -.
DR SMR; Q0TMV4; -.
DR STRING; 195103.CPF_2656; -.
DR EnsemblBacteria; ABG83930; ABG83930; CPF_2656.
DR GeneID; 29570235; -.
DR KEGG; cpf:CPF_2656; -.
DR eggNOG; COG3426; Bacteria.
DR HOGENOM; CLU_048716_0_0_9; -.
DR OMA; IWHALNQ; -.
DR OrthoDB; 537106at2; -.
DR UniPathway; UPA00863; -.
DR Proteomes; UP000001823; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047761; F:butyrate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019605; P:butyrate metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00542; Butyrate_kinase; 1.
DR InterPro; IPR000890; Aliphatic_acid_kin_short-chain.
DR InterPro; IPR023865; Aliphatic_acid_kinase_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR011245; Butyrate_kin.
DR PANTHER; PTHR21060; PTHR21060; 1.
DR PANTHER; PTHR21060:SF3; PTHR21060:SF3; 1.
DR Pfam; PF00871; Acetate_kinase; 1.
DR PIRSF; PIRSF036458; Butyrate_kin; 1.
DR PRINTS; PR00471; ACETATEKNASE.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR02707; butyr_kinase; 1.
DR PROSITE; PS01075; ACETATE_KINASE_1; 1.
DR PROSITE; PS01076; ACETATE_KINASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..356
FT /note="Butyrate kinase"
FT /id="PRO_0000273580"
SQ SEQUENCE 356 AA; 38703 MW; 43D4FBAC1032D87F CRC64;
MAYKLLIINP GSTSTKIGVY EGEKEILEET LRHSAEEILK YDTIFDQLDF RKEVILKVLK
EKGIDINELD AVVGRGGMLK PIEGGTYEVN EAMVEDLKIG VQGPHASNLG GILSNEIAKE
IGKRAFIVDP VVVDEMEDVA RLSGVPELPR KSKFHALNQK AVAKRYAKEH NTSYEDVNLI
VVHMGGGVSV GAHRKGRVID VNNALDGDGP FSPERAGGVP SGELLEMCFS GKYSKEEVYK
KLVGKGGFVA YANTNDARDL IKLSQEGDEK GSLIFNAFIY QIAKEIGSMA VVLDGEVDAI
VLTGGIAYSD YVTNAINKKV KWIAPMVVYG GEDELLALAQ GAIRVLDGVE EAKIYK