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Entry: A0A2S5BFW5_9BASI
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ID   A0A2S5BFW5_9BASI        Unreviewed;       445 AA.
AC   A0A2S5BFW5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Probable acetate kinase {ECO:0000256|HAMAP-Rule:MF_03131};
DE            EC=2.7.2.1 {ECO:0000256|HAMAP-Rule:MF_03131};
DE   AltName: Full=Acetokinase {ECO:0000256|HAMAP-Rule:MF_03131};
GN   ORFNames=BMF94_1289 {ECO:0000313|EMBL:POY75666.1};
OS   Rhodotorula taiwanensis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=741276 {ECO:0000313|EMBL:POY75666.1, ECO:0000313|Proteomes:UP000237144};
RN   [1] {ECO:0000313|EMBL:POY75666.1, ECO:0000313|Proteomes:UP000237144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD1149 {ECO:0000313|EMBL:POY75666.1,
RC   ECO:0000313|Proteomes:UP000237144};
RX   PubMed=29375494;
RA   Tkavc R., Matrosova V.Y., Grichenko O.E., Gostincar C., Volpe R.P.,
RA   Klimenkova P., Gaidamakova E.K., Zhou C.E., Stewart B.J., Lyman M.G.,
RA   Malfatti S.A., Rubinfeld B., Courtot M., Singh J., Dalgard C.L.,
RA   Hamilton T., Frey K.G., Gunde-Cimerman N., Dugan L., Daly M.J.;
RT   "Prospects for Fungal Bioremediation of Acidic Radioactive Waste Sites:
RT   Characterization and Genome Sequence of Rhodotorula taiwanensis MD1149.";
RL   Front. Microbiol. 8:2528-2528(2018).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP = acetyl phosphate + ADP; Xref=Rhea:RHEA:11352,
CC         ChEBI:CHEBI:22191, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:456216; EC=2.7.2.1; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03131};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03131};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC       acetyl-CoA from acetate: step 1/2. {ECO:0000256|HAMAP-Rule:MF_03131}.
CC   -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_03131}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03131}.
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:POY75666.1}.
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DR   EMBL; PJQD01000013; POY75666.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S5BFW5; -.
DR   STRING; 741276.A0A2S5BFW5; -.
DR   OrthoDB; 21304at2759; -.
DR   UniPathway; UPA00340; UER00458.
DR   Proteomes; UP000237144; Unassembled WGS sequence.
DR   GO; GO:0008776; F:acetate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006082; P:organic acid metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_00020; Acetate_kinase; 1.
DR   InterPro; IPR004372; Ac/propionate_kinase.
DR   InterPro; IPR000890; Aliphatic_acid_kin_short-chain.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR21060; ACETATE KINASE; 1.
DR   PANTHER; PTHR21060:SF19; ACETATE KINASE; 1.
DR   Pfam; PF00871; Acetate_kinase; 1.
DR   PIRSF; PIRSF000722; Acetate_prop_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_03131}; Kinase {ECO:0000256|HAMAP-Rule:MF_03131};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_03131};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03131};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_03131}; Reference proteome {ECO:0000313|Proteomes:UP000237144};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03131}.
FT   ACT_SITE        162
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT   BINDING         17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT   BINDING         223..227
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT   BINDING         427
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT   SITE            195
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT   SITE            256
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
SQ   SEQUENCE   445 AA;  48915 MW;  72A06EE8943B5F3B CRC64;
     MPADLDLAVN CGSSSIKFSL YSASSRKLVV SGSANNVQGD SPAQYEFTFQ RDEGKENKKE
     REIDGKTTYE EIFTKILEDV TSDEVLGKEG KTRIRLVAHR IVHGGTADAP IVIRHGDKDE
     QATLDQMDAV SDFAPLHNHH AMLIVKECLE HLPEAYSVLC FDTLFHQTIP QYRRTYAISQ
     PEHKTPVPLV KYGFHGLSYA NIRDQMAEQL GKPKDQVNLV VAHLGSGGSC CLIRNGKSVQ
     TTMGVTPLEG LPGGTRSGTL DPSLIFHHTP DCSTTVKWSG RDISKAEYVL NKESGFKALC
     GTNNFGTITS RAFPSEGDKE QPSNEDHMSS RLTYQLYLDH LLAFLSGYIT DTLSSPEGRL
     DALVFSGGIG ERSSRLRADV LARFRFVEEL ASSGGGLDVD ANEKGKGRRR ITREGSKVPA
     WVVETSEEDE MVRMAEEALQ EGSAK
//
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