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Database: UniProt
Entry: A0A0C7NZZ8_DEFTU
LinkDB: A0A0C7NZZ8_DEFTU
Original site: A0A0C7NZZ8_DEFTU 
ID   A0A0C7NZZ8_DEFTU        Unreviewed;       362 AA.
AC   A0A0C7NZZ8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
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   ECO:0000313|EMBL:CEP78863.1};
GN   ORFNames=DTL3_1574 {ECO:0000313|EMBL:CEP78863.1};
OS   Defluviitoga tunisiensis.
OC   Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC   Defluviitoga.
OX   NCBI_TaxID=1006576 {ECO:0000313|EMBL:CEP78863.1, ECO:0000313|Proteomes:UP000032809};
RN   [1] {ECO:0000313|Proteomes:UP000032809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L3 {ECO:0000313|Proteomes:UP000032809};
RA   Wibberg D.;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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|HAMAP-Rule:MF_00542};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00542}.
CC   -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00542, ECO:0000256|RuleBase:RU003835}.
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DR   EMBL; LN824141; CEP78863.1; -; Genomic_DNA.
DR   RefSeq; WP_045088231.1; NZ_LN824141.1.
DR   AlphaFoldDB; A0A0C7NZZ8; -.
DR   STRING; 1006576.DTL3_1574; -.
DR   KEGG; dtn:DTL3_1574; -.
DR   PATRIC; fig|1006576.9.peg.1570; -.
DR   HOGENOM; CLU_048716_0_0_0; -.
DR   OrthoDB; 9771859at2; -.
DR   Proteomes; UP000032809; Chromosome I.
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; 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.
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|HAMAP-Rule:MF_00542, ECO:0000256|RuleBase:RU003835};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00542}; Reference proteome {ECO:0000313|Proteomes:UP000032809};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00542}.
SQ   SEQUENCE   362 AA;  40642 MW;  001B63971DD3F8C6 CRC64;
     MKKILVIYPD WNVTKIALFE GENKLLEKII THDKTILLTY ESIIDQFNYR KKQVIHSLNQ
     LCISINELDA IAARGGVLSP MPSGTYIVNE TIVDYLRTKS PIEHPANLGA LIAFDLSETS
     NKKPPVFMTD PLSVDEFVPE ARIAGVPQLE RISRYNALNM KTVARYASNK LKKDYWDCNF
     VIAHLDKHIS IGAHRKGLMI DVTYPFDEGP FGLHTTGDLP LVDLTTWIFK HMNEYSENEI
     KKRFIENGGL LAYLGTSELD EAVEKGITDK NAKLIVEAMA YQIAKEIGAM AAVLGGDIDA
     VLLTGEIINN ECFVRLVKNK IAKLGIVMLY PGSYELEGLA YGALRVLYQL EEFLVWKGEK
     VT
//
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