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BUK_CLOB8
ID   BUK_CLOB8               Reviewed;         355 AA.
AC   Q05619; A6LPW4;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Butyrate kinase;
DE            Short=BK;
DE            EC=2.7.2.7;
GN   Name=buk; OrderedLocusNames=Cbei_0204;
OS   Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS   acetobutylicum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=290402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8396545; DOI=10.1016/0378-1119(93)90677-u;
RA   Oultram J.D., Burr I.D., Elmore M.J., Minton N.P.;
RT   "Cloning and sequence analysis of the genes encoding phosphotransbutyrylase
RT   and butyrate kinase from Clostridium acetobutylicum NCIMB 8052.";
RL   Gene 131:107-112(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA   Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA   Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA   Blaschek H., Richardson P.;
RT   "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of butyryl-CoA through butyryl
CC       phosphate to butyrate.
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   -!- MISCELLANEOUS: Also acts, albeit more slowly, on pentanoate and
CC       propanoate, and on some branched-chain fatty acids.
CC   -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000305}.
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DR   EMBL; L04468; AAA52081.1; -; Genomic_DNA.
DR   EMBL; CP000721; ABR32394.1; -; Genomic_DNA.
DR   RefSeq; WP_011967556.1; NC_009617.1.
DR   AlphaFoldDB; Q05619; -.
DR   SMR; Q05619; -.
DR   STRING; 290402.Cbei_0204; -.
DR   EnsemblBacteria; ABR32394; ABR32394; Cbei_0204.
DR   KEGG; cbe:Cbei_0204; -.
DR   eggNOG; COG3426; Bacteria.
DR   HOGENOM; CLU_048716_0_0_9; -.
DR   OMA; ANDEGPF; -.
DR   OrthoDB; 537106at2; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000000565; 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..355
FT                   /note="Butyrate kinase"
FT                   /id="PRO_0000107659"
SQ   SEQUENCE   355 AA;  38434 MW;  1CA92F594D7CB0E4 CRC64;
     MSYKLLIINP GSTSTKIGVY EGEKELFEET LRHTNEEIKR YDTIYDQFEF RKEVILNVLK
     EKNFDIKTLS AIVGRGGMLR PVEGGTYAVN DAMVEDLKVG VQGPHASNLG GIIAKSIGDE
     LNIPSFIVDP VVTDELADVA RLSGVPELPR KSKFHALNQK AVAKRYGKES GQGYENLNLV
     VVHMGGGVSV GAHNHGKVVD VNNALDGDGP FSPERAGSVP IGDLVKMCFS GKYSEAEVYG
     KAVGKGGFVG YLNTNDVKGV IDKMEEGDKE CESIYKAFVY QISKAIGEMS VVLEGKVDQI
     IFTGGIAYSP TLVPDLKAKV EWIAPVTVYP GEDELLALAQ GAIRVLDGEE QAKVY
 
 
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