ID A0A1D2KB99_BROTH Unreviewed; 366 AA.
AC A0A1D2KB99;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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:ATF26615.1};
GN ORFNames=CNY62_09585 {ECO:0000313|EMBL:ATF26615.1};
OS Brochothrix thermosphacta (Microbacterium thermosphactum).
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Brochothrix.
OX NCBI_TaxID=2756 {ECO:0000313|EMBL:ATF26615.1, ECO:0000313|Proteomes:UP000243591};
RN [1] {ECO:0000313|EMBL:ATF26615.1, ECO:0000313|Proteomes:UP000243591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BI {ECO:0000313|EMBL:ATF26615.1,
RC ECO:0000313|Proteomes:UP000243591};
RA Paoli G.C., Wijey C., Chen C.-Y., Nguyen L., Yan X., Irwin P.L.;
RT "Complete Genome Sequences of Two Strains of the Meat Spoilage Bacterium
RT Brochothrix thermosphacta Isolated from Ground Chicken.";
RL Submitted (SEP-2017) 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; CP023483; ATF26615.1; -; Genomic_DNA.
DR RefSeq; WP_029091151.1; NZ_RSDU01000023.1.
DR AlphaFoldDB; A0A1D2KB99; -.
DR STRING; 2756.BFR44_11210; -.
DR GeneID; 66536671; -.
DR KEGG; bths:CNY62_09585; -.
DR OrthoDB; 9771859at2; -.
DR Proteomes; UP000243591; 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; 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:UP000243591};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00542}.
SQ SEQUENCE 366 AA; 40841 MW; 16002B5E5279CF7F CRC64;
MLGKKRILII NTGVQSIKIA IFDEDKVVFN KTIREQKVQP INDYITLQKQ LTATKQRLLL
QLKKAKIEMK SIDLIVSNTG YIQPVKSGAY TINEAMVSDL IEHSFYEAEG SFGAILAHSL
AEYYQVPAIT YDPPTVDELQ DVARVSGHPD FVRRSYFNAL NQKAVGRHIA KKIGTTYEEA
KFIIVHLGSA VSVGAHENGK VIDVNNGYYG EGPFSTIRTG SLPMEAVMKK YIASPEEVKE
LPLILKQGGF LGYLGTDSLT DVEWRIVEDD QEAIAIYDAM TYQIAKEIGA YATVLKGNVD
AVILTGGMSI SPFLVKKISE YIKWIAPIHI VEDQLEMQTL SQVGLRVLNN EEEVMMYTSC
DAKRHK
//
