ID A0A267MKZ2_9CLOT Unreviewed; 356 AA.
AC A0A267MKZ2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 ECO:0000313|EMBL:PAB60206.1};
GN ORFNames=CCE28_04720 {ECO:0000313|EMBL:PAB60206.1};
OS Anaeromicrobium sediminis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Anaeromicrobium.
OX NCBI_TaxID=1478221 {ECO:0000313|EMBL:PAB60206.1, ECO:0000313|Proteomes:UP000216024};
RN [1] {ECO:0000313|EMBL:PAB60206.1, ECO:0000313|Proteomes:UP000216024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY2726D {ECO:0000313|EMBL:PAB60206.1,
RC ECO:0000313|Proteomes:UP000216024};
RA Zeng X.;
RT "Draft genome sequence of anaerobic fermentative bacterium Anaeromicrobium
RT sediminis DY2726D isolated from West Pacific Ocean sediments.";
RL Submitted (JUN-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:PAB60206.1}.
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DR EMBL; NIBG01000003; PAB60206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267MKZ2; -.
DR OrthoDB; 9771859at2; -.
DR Proteomes; UP000216024; 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}; Reference proteome {ECO:0000313|Proteomes:UP000216024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00542}.
SQ SEQUENCE 356 AA; 38614 MW; 86671C9F47FBCE9D CRC64;
MKYRILTINP GSTSTKIGVF DGDELVFEET LRHSSEEIGQ FKKIYDQYNF RKEVILNVLK
ENAIKLESLN ACVGRGGLLK PIAGGTYEVN DPMIEDLKVG VLGQHASNLG GIIAKEIAKD
LNIKAYIVDP VVVDEMIDLA RVSGMPEYDR MSIFHALNQK AVARKAAKEL GKKYDELNFV
VAHLGGGISV GAHELGKVID VNNALDGEGP FSPERSGTVP VRKIMKMAFS GEYTVEEFNK
KVSGKGGLVA YLNTNDGRDV KKMVAAGNAQ AGVIYQAMAY QVAKEIGSMC VALGGKVDGI
ILTGGIAYDS EFVGWIKERA EFLGKVFVYP GEEELRALAE GGLRVLKGEE EAKVYA
//
