ID A0A1W9VU26_9BACT Unreviewed; 357 AA.
AC A0A1W9VU26;
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=B6226_00965 {ECO:0000313|EMBL:OQY39895.1};
OS Candidatus Cloacimonetes bacterium 4572_65.
OC Bacteria; Candidatus Cloacimonadota.
OX NCBI_TaxID=1972455 {ECO:0000313|EMBL:OQY39895.1, ECO:0000313|Proteomes:UP000231707};
RN [1] {ECO:0000313|EMBL:OQY39895.1, ECO:0000313|Proteomes:UP000231707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4572_65 {ECO:0000313|EMBL:OQY39895.1};
RX PubMed=28835260; DOI=.1186/s40168-017-0322-2;
RA Dombrowski N., Seitz K.W., Teske A.P., Baker B.J.;
RT "Genomic insights into potential interdependencies in microbial hydrocarbon
RT and nutrient cycling in hydrothermal sediments.";
RL Microbiome 5:106-106(2017).
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:OQY39895.1}.
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DR EMBL; NBMD01000011; OQY39895.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9VU26; -.
DR Proteomes; UP000231707; 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 CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
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 357 AA; 38776 MW; 0590E0C45BCE4AD1 CRC64;
MENRVLAINP GSTSTKIAVY DDTKEVFTTT LRHDAEALEA FGGIIEQYDY RKNLVLEAMK
ENNVAPETLS AVVGRGGLMK SIPGGTYTVN EKMKKDLSDP ALWGRIHASN LGAFISESIA
NDFNIKSFIV DPVVVDEFDD IARISGIPEI ERQSLFHALN IRYIARLLAE KLGKELSECN
MIGIHMGGGI SIAAIKGGRV VDVNNALLGM GAFSPQRAGA LPIGDLIDMC YSGDYTKKEL
QGYLSKKAGY VAYLGTDDGR EVGEMIENGN EKARLIQDAM CYQVAKEVGA CATVMNGKVD
LIFMSGGLVY NKLIVKTISD RVGFIAPIEL FPGEKEMEAL CQGGVRVLKG LEEAKIY
//
