ID A0A101F9S9_9THEM Unreviewed; 375 AA. AC A0A101F9S9; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 13-NOV-2019, entry version 16. 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 ORFNames=XD64_1114 {ECO:0000313|EMBL:KUK33058.1}; OS Thermotoga sp. 47_83. OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga; OC unclassified Thermotoga. OX NCBI_TaxID=1635261 {ECO:0000313|EMBL:KUK33058.1}; RN [1] {ECO:0000313|EMBL:KUK33058.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=47_83 {ECO:0000313|EMBL:KUK33058.1}; RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M., RA Andersen G.L., Banfield J.F.; RT "Genome-resolved metagenomic analysis reveals roles for candidate RT phyla and other microbial community members in biogeochemical RT transformations in oil reservoirs."; RL MBio 7:e01669-15(2015). 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, CC ECO:0000256|SAAS:SAAS00688878}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUK33058.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LGFM01000121; KUK33058.1; -; Genomic_DNA. DR PATRIC; fig|1635261.3.peg.510; -. 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 HAMAP; MF_00542; Butyrate_kinase; 1. DR InterPro; IPR000890; Aliphatic_acid_kin_short-chain. DR InterPro; IPR023865; Aliphatic_acid_kinase_CS. 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 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 {ECO:0000256|HAMAP-Rule:MF_00542, KW ECO:0000256|SAAS:SAAS00130545}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00542}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00542, KW ECO:0000256|RuleBase:RU003835, ECO:0000256|SAAS:SAAS00130569, KW ECO:0000313|EMBL:KUK33058.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00542, KW ECO:0000256|SAAS:SAAS00130625}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00542, KW ECO:0000256|RuleBase:RU003835, ECO:0000256|SAAS:SAAS00130632}. SQ SEQUENCE 375 AA; 42184 MW; CF95CABE10BA1605 CRC64; MFRILTINPG STSTKLSIFE DERMVKMQNF SHSPDELGRF QRILDQLEFR EKIVRQFVEE TGYSLSSFSA FVSRGGLLDP IPGGVYLVDD LMIETLKSAK NGEHASNLGV IIAHRFSAET GVPAYVVDPV VVDEMEDFAR VSGHPNYQRK SIFHALNQKA VAKEVARMMN KRYEEMNLVV AHMGGGISIA AHRKGRVIDV NNALDGDGPF TPERSGTLPL TQLVDLCFSG KFTYEEMKKR IVGNGGLVAY LGTSDAREVV RRIKQGDEWA KRVYRAMAYQ IAKWIGKMAA VLKGEVDFIV LTGGLAHEKE FLVPWITERV SFIAPVLVFP GSNEEKALAL SALRVLRGEE NLKNYSEESR RWRERYDSYL DGILR //