BUK_COPPD
ID BUK_COPPD Reviewed; 356 AA.
AC B5Y8N2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Probable butyrate kinase {ECO:0000255|HAMAP-Rule:MF_00542};
DE Short=BK {ECO:0000255|HAMAP-Rule:MF_00542};
DE EC=2.7.2.7 {ECO:0000255|HAMAP-Rule:MF_00542};
DE AltName: Full=Branched-chain carboxylic acid kinase {ECO:0000255|HAMAP-Rule:MF_00542};
GN Name=buk {ECO:0000255|HAMAP-Rule:MF_00542};
GN OrderedLocusNames=COPRO5265_0782;
OS Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / OCM 4 /
OS BT).
OC Bacteria; Coprothermobacterota; Coprothermobacteria; Coprothermobacterales;
OC Coprothermobacteraceae; Coprothermobacter.
OX NCBI_TaxID=309798;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35245 / DSM 5265 / OCM 4 / BT;
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Coprothermobacter proteolyticus strain
RT ATCC 5245 / DSM 5265 / BT.";
RL Submitted (AUG-2008) 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:0000255|HAMAP-Rule:MF_00542};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00542}.
CC -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00542}.
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DR EMBL; CP001145; ACI18124.1; -; Genomic_DNA.
DR RefSeq; WP_012544774.1; NC_011295.1.
DR AlphaFoldDB; B5Y8N2; -.
DR SMR; B5Y8N2; -.
DR STRING; 309798.COPRO5265_0782; -.
DR EnsemblBacteria; ACI18124; ACI18124; COPRO5265_0782.
DR KEGG; cpo:COPRO5265_0782; -.
DR eggNOG; COG3426; Bacteria.
DR HOGENOM; CLU_048716_0_0_9; -.
DR OMA; IWHALNQ; -.
DR OrthoDB; 537106at2; -.
DR Proteomes; UP000001732; 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 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; Reference proteome;
KW Transferase.
FT CHAIN 1..356
FT /note="Probable butyrate kinase"
FT /id="PRO_1000128904"
SQ SEQUENCE 356 AA; 38667 MW; E195C6CC80AD5482 CRC64;
MGFQILTINP GSTSTKVAWF DDDKLVWKDS VEHDAVTLSQ FPSIAAQFEL RASEVEKAVE
KHGSDLNTLD AVVGRGGLLR PISSGVYSVN ETMLKELIDA RYGEHASNLG APIAHAIASK
VGCPAFIVDP VVVDEMDDIS RLSGWPELPR KSIFHALNQK AVARRVARDF FSVPYEQLNL
IVAHLGGGIS IGAHKKGRVV DVNNALGGEG PMSPERAGTL PIMKLADYLY EHKPDRKEFS
KKLVGKGGWV AHLGTNSGKD LEERVKNGDE HAILILKATG YQISKWIAQM AVALAGEVDG
IIITGGLAYI PELVDFIQER VLWIAPVFVV PGEDEMLALA EGALRVLRGQ EEAKTY
