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Database: UniProt
Entry: F6DLF8_DESRL
LinkDB: F6DLF8_DESRL
Original site: F6DLF8_DESRL 
ID   F6DLF8_DESRL            Unreviewed;       354 AA.
AC   F6DLF8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Probable butyrate kinase {ECO:0000256|HAMAP-Rule:MF_00542};
DE            Short=BK {ECO:0000256|HAMAP-Rule:MF_00542};
DE            EC=2.7.2.7 {ECO:0000256|HAMAP-Rule:MF_00542};
DE   AltName: Full=Branched-chain carboxylic acid kinase {ECO:0000256|HAMAP-Rule:MF_00542};
GN   Name=buk {ECO:0000256|HAMAP-Rule:MF_00542};
GN   OrderedLocusNames=Desru_2257 {ECO:0000313|EMBL:AEG60506.1};
OS   Desulforamulus ruminis (strain ATCC 23193 / DSM 2154 / NCIMB 8452 / DL)
OS   (Desulfotomaculum ruminis).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=696281 {ECO:0000313|EMBL:AEG60506.1, ECO:0000313|Proteomes:UP000009234};
RN   [1] {ECO:0000313|Proteomes:UP000009234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23193 / DSM 2154 / NCIB 8452 / DL
RC   {ECO:0000313|Proteomes:UP000009234};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Mikhailova N., Pagani I., Stams A.J.M., Plugge C.M., Muyzer G.,
RA   Kuever J., Parshina S.N., Ivanova A.E., Nazina T.N., Brambilla E.,
RA   Spring S., Klenk H.-P., Woyke T.;
RT   "Complete sequence of Desulfotomaculum ruminis DSM 2154.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEG60506.1, ECO:0000313|Proteomes:UP000009234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23193 / DSM 2154 / NCIB 8452 / DL
RC   {ECO:0000313|Proteomes:UP000009234};
RX   PubMed=23408247; DOI=10.4056/sigs.3226659;
RA   Spring S., Visser M., Lu M., Copeland A., Lapidus A., Lucas S., Cheng J.F.,
RA   Han C., Tapia R., Goodwin L.A., Pitluck S., Ivanova N., Land M., Hauser L.,
RA   Larimer F., Rohde M., Goker M., Detter J.C., Kyrpides N.C., Woyke T.,
RA   Schaap P.J., Plugge C.M., Muyzer G., Kuever J., Pereira I.A.,
RA   Parshina S.N., Bernier-Latmani R., Stams A.J., Klenk H.P.;
RT   "Complete genome sequence of the sulfate-reducing firmicute
RT   Desulfotomaculum ruminis type strain (DL(T)).";
RL   Stand. Genomic Sci. 7:304-319(2012).
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         Evidence={ECO:0000256|ARBA:ARBA00001819, ECO:0000256|HAMAP-
CC         Rule:MF_00542};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00542}.
CC   -!- SIMILARITY: Belongs to the acetokinase family.
CC       {ECO:0000256|ARBA:ARBA00008748, ECO:0000256|HAMAP-Rule:MF_00542,
CC       ECO:0000256|RuleBase:RU003835}.
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DR   EMBL; CP002780; AEG60506.1; -; Genomic_DNA.
DR   RefSeq; WP_013842265.1; NC_015589.1.
DR   AlphaFoldDB; F6DLF8; -.
DR   STRING; 696281.Desru_2257; -.
DR   KEGG; dru:Desru_2257; -.
DR   eggNOG; COG3426; Bacteria.
DR   HOGENOM; CLU_048716_0_0_9; -.
DR   OrthoDB; 9771859at2; -.
DR   Proteomes; UP000009234; 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:0016310; P:phosphorylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.420.40; -; 2.
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   NCBIfam; TIGR02707; butyr_kinase; 1.
DR   PANTHER; PTHR21060; ACETATE KINASE; 1.
DR   PANTHER; PTHR21060:SF3; BUTYRATE KINASE 2-RELATED; 1.
DR   Pfam; PF00871; Acetate_kinase; 1.
DR   PIRSF; PIRSF036458; Butyrate_kin; 1.
DR   PRINTS; PR00471; ACETATEKNASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS01075; ACETATE_KINASE_1; 1.
DR   PROSITE; PS01076; ACETATE_KINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00542};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00542};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00542};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00542}; Reference proteome {ECO:0000313|Proteomes:UP000009234};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00542}.
SQ   SEQUENCE   354 AA;  38345 MW;  0635A8D43E893764 CRC64;
     MLILAINPGS TSTKIAAFQG KQGLWKETIE HSVEEVGSFS KITDQSGFRT ATILNILKKR
     GCEMGQFSAV VGRGGLLKPL VGGTYRVDEY LVNELQNAPE GEHASNLGGI IAYQLAQSVS
     VPAYIVDPVA VDELEPHARL SGHPEIPRVS LSHALNMKAV ARKVAAQRGK DYREMNLLMA
     HLGGGISVAA HRKGRMIDVN NANAEGPFSP ERCGTLPSRQ LVKLCFSGRY NQEEMFTLLN
     KEGGMYAYLG IKDVREAEKR MAGGDEQARL VLEAMCYQVA KEIGAMSAVL AGEVECIVLT
     GGIAYSDFIT GEIVRRVSFI APVVVVPGEE EMESLALGAL RVLQHEEEAL TYRA
//
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