ID A0A3G8YE80_9DEIO Unreviewed; 365 AA.
AC A0A3G8YE80;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=EHF33_13410 {ECO:0000313|EMBL:AZI43622.1};
OS Deinococcus psychrotolerans.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=2489213 {ECO:0000313|EMBL:AZI43622.1, ECO:0000313|Proteomes:UP000276417};
RN [1] {ECO:0000313|EMBL:AZI43622.1, ECO:0000313|Proteomes:UP000276417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14-83T {ECO:0000313|EMBL:AZI43622.1,
RC ECO:0000313|Proteomes:UP000276417};
RA Tian J.;
RT "Deinococcus shelandsis sp. nov., isolated from South Shetland Islands soil
RT of Antarctica.";
RL Submitted (NOV-2018) 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; CP034183; AZI43622.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G8YE80; -.
DR KEGG; dph:EHF33_13410; -.
DR OrthoDB; 9771859at2; -.
DR Proteomes; UP000276417; Chromosome 1.
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 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00542}.
SQ SEQUENCE 365 AA; 38636 MW; 09E5251A9E5BC19A CRC64;
MLAYVINPGS TSTKLALAEI ERGDNPALPS LLRLKLDKTE VMHSALLSGP LELGDLQADL
MTAATDWPKP DAVVAACGLI GNLQAGAYRV TPELAEWLLT HPHGEYTSNV GAALALHLAE
SRGVPAYVVD PPDVDELRPE ARVSGLAGVE RLSRLHTLNA RLVARRAAHE QGLRFQDARV
VVAHLGGSIS VSAFEGAKII DTTGARLDEG PFTPSRAGTL PIRALLDVAY SRPRSDAEKL
LLSGAGFLGL TGTADLRELE RREKTESRVK LAADAFAYQV AKNIGAYSAA LSARPHAVAI
TGGIARWESV VNRIERQIGW IAPLTVLPGD LELEALAEGM GRVLLGLETA QDWTPPGAAS
AADSV
//
