ID A0A0A8WHC7_PAESO Unreviewed; 367 AA.
AC A0A0A8WHC7;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 50.
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_2 {ECO:0000313|EMBL:CEQ05204.1};
GN Synonyms=buk {ECO:0000256|HAMAP-Rule:MF_00542};
GN ORFNames=R28058_29211 {ECO:0000313|EMBL:CEQ05204.1};
OS Paeniclostridium sordellii (Clostridium sordellii).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Paeniclostridium.
OX NCBI_TaxID=1505 {ECO:0000313|EMBL:CEQ05204.1, ECO:0000313|Proteomes:UP000049127};
RN [1] {ECO:0000313|EMBL:CEQ05204.1, ECO:0000313|Proteomes:UP000049127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R28058 {ECO:0000313|EMBL:CEQ05204.1,
RC ECO:0000313|Proteomes:UP000049127};
RA Aslett A.Martin., De Silva Nishadi;
RL Submitted (JAN-2015) 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}.
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DR EMBL; CEKZ01000024; CEQ05204.1; -; Genomic_DNA.
DR RefSeq; WP_021127420.1; NZ_WQMV01000006.1.
DR AlphaFoldDB; A0A0A8WHC7; -.
DR PATRIC; fig|1505.7.peg.3038; -.
DR eggNOG; COG3426; Bacteria.
DR OrthoDB; 9771859at2; -.
DR Proteomes; UP000049127; 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 367 AA; 39670 MW; 8C88E91301D64906 CRC64;
MEKKFKILTI NPGSTSTKIA VFDNEELLFE KTLRHTSEEI SKYQKISDQF EFRKKVIEDA
LKEGGISTSE LDAVVGRGGL LKPITGGTYS VDDEMIEDLK VGVLGEHASN LGGLIAKEIG
DSVGIPSYIV DPVVVDELND VARISGMPEI TRKSIFHALN QKATARRAAK DLNKKYEDCN
FIVAHMGGGI SVGAHLKGSV IDVANALDGE GPFSPERSGG LPVGDLVKMC FSGEYTQEDI
KKRIKGNGGL VAYLNTNDGR EVEAMIEEGN EKAKIVYEAM AYQVAKEIGA CAAVLNGEVD
AVLLTGGIAY SKMFTNMIID RIKFVAQAKV YPGEDEMIAL AQGGLRVLMK EEEAKIYGKE
LALANTL
//
