ID A0A1W9S0A4_9BACT Unreviewed; 377 AA.
AC A0A1W9S0A4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=B6D57_03945 {ECO:0000313|EMBL:OQX90281.1};
OS Candidatus Coatesbacteria bacterium 4484_99.
OC Bacteria; Candidatus Coatesbacteria.
OX NCBI_TaxID=1970774 {ECO:0000313|EMBL:OQX90281.1, ECO:0000313|Proteomes:UP000192611};
RN [1] {ECO:0000313|Proteomes:UP000192611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dombrowski N., Seitz K., Teske A., Baker B.;
RT "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT hydrothermal sediment communities.";
RL Submitted (MAR-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|ARBA:ARBA00001819, ECO:0000256|HAMAP-
CC Rule:MF_00542};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00542}.
CC -!- SIMILARITY: Belongs to the acetokinase family.
CC {ECO:0000256|ARBA:ARBA00008748, ECO:0000256|HAMAP-Rule:MF_00542,
CC ECO:0000256|RuleBase:RU003835}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQX90281.1}.
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; NATQ01000076; OQX90281.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9S0A4; -.
DR Proteomes; UP000192611; Unassembled WGS sequence.
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; IPR023865; Aliphatic_acid_kinase_CS.
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.
DR PROSITE; PS01075; ACETATE_KINASE_1; 1.
DR PROSITE; PS01076; ACETATE_KINASE_2; 1.
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|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00542};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00542};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00542}.
SQ SEQUENCE 377 AA; 41838 MW; D3FC10EFF95C8962 CRC64;
MTEKNNLYIL TINPGSTSTK IAIYEDSKAI FEEEIMHDPE VVMSFKKRDE DYRFRKETIL
GLLSEKGFDI NKFSAVVGRG GFVQPIEGGV YEVNRKMLDD LEHRAPYEHP SNLGAPLAYE
IASGIGVKAY TVDPVVVDEM SDLARVSGYP GIIRKSVLHA LNIRAVARIA AEKHLKKKHS
DVNLIVIHMG GGISVTAHFR GKMVDVNNAF LGMGPFTPQR VGALPTGELI KLCYSGKFTQ
KELEAELVKN AGLRGYLGTN DAIEIEKMIE NGNELARLIY EALAYQISKE VGAMATVLKG
NVDAIIFTGG LSRSDMLMRW IKERVSFIAD VIVIPGQKEM DAMAESVLRI LKGEEEAKEY
IPKEILDPMK KYGKQEV
//
