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
//