GenomeNet

Database: UniProt
Entry: A0A1Y1CHU1_9BACT
LinkDB: A0A1Y1CHU1_9BACT
Original site: A0A1Y1CHU1_9BACT 
ID   A0A1Y1CHU1_9BACT        Unreviewed;       357 AA.
AC   A0A1Y1CHU1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-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=ALGA_1551 {ECO:0000313|EMBL:BAX79927.1};
OS   Labilibaculum antarcticum.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae;
OC   Labilibaculum.
OX   NCBI_TaxID=1717717 {ECO:0000313|EMBL:BAX79927.1, ECO:0000313|Proteomes:UP000218267};
RN   [1] {ECO:0000313|Proteomes:UP000218267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPP2 {ECO:0000313|Proteomes:UP000218267};
RA   Watanabe M., Kojima H., Fukui M.;
RT   "Complete genome sequence of Marinifilaceae bacterium strain SPP2, isolated
RT   from the Antarctic marine sediment.";
RL   Mar. Genomics 0:0-0(2017).
RN   [2] {ECO:0000313|EMBL:BAX79927.1, ECO:0000313|Proteomes:UP000218267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPP2 {ECO:0000313|EMBL:BAX79927.1,
RC   ECO:0000313|Proteomes:UP000218267};
RA   Watanabe M., Kojima H., Fukui M.;
RT   "Complete genome sequence of Marinifilaceae bacterium strain SPP2, isolated
RT   from the Antarctic marine sediment.";
RL   Mar. Genomics 39:1-2(2018).
RN   [3] {ECO:0000313|Proteomes:UP000218267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPP2 {ECO:0000313|Proteomes:UP000218267};
RA   Watanabe M., Kojima H., Fukui M.;
RT   "Labilibaculum antarcticum sp. nov., a novel facultative anaerobic,
RT   psychrotorelant bacterium isolated from marine sediment of Antarctica.";
RL   Antonie Van Leeuwenhoek 113:349-355(2020).
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   ---------------------------------------------------------------------------
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; AP018042; BAX79927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1CHU1; -.
DR   KEGG; mbas:ALGA_1551; -.
DR   Proteomes; UP000218267; 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; 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.
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;  39390 MW;  DCC7F710C20BFEE0 CRC64;
     MNSNEIVIVI NPGSTSTKIA LYNRTELINE LIVRHSQVDL DQFQKVTDQF EYRYQMVEDG
     LDEMLSKEDL HVVGIVGRGG IVKPLEGGTY RINNSFLEDA KTGKYGDHAS NLGSMLANKL
     AKHFNLDESF TVDPVSAGNI WEKARISGVP GIERNRRGHP LNMKMTARKT AKQQNITFEE
     AKYVIAHLGG GISIASVDGG KIVDVNDALM GMGPFSPNRA GALPSRGVMD LCYSMPRNEV
     EALLSKNSGL KAYLGVDDLR DVFKLIDSGN EKAQLIYDAF VYQIAKEIGA YHVALKCKAN
     GIIITGGIAY SERFISDLKT YVEKLTNFFV YPGENEMEAL AEGAFRVIDG KEMALEY
//
DBGET integrated database retrieval system