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Database: UniProt
Entry: A0A1C7M578_GRIFR
LinkDB: A0A1C7M578_GRIFR
Original site: A0A1C7M578_GRIFR 
ID   A0A1C7M578_GRIFR        Unreviewed;       279 AA.
AC   A0A1C7M578;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   22-FEB-2023, entry version 20.
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=A0H81_07866 {ECO:0000313|EMBL:OBZ72095.1};
OS   Grifola frondosa (Maitake) (Polyporus frondosus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Grifolaceae; Grifola.
OX   NCBI_TaxID=5627 {ECO:0000313|EMBL:OBZ72095.1, ECO:0000313|Proteomes:UP000092993};
RN   [1] {ECO:0000313|EMBL:OBZ72095.1, ECO:0000313|Proteomes:UP000092993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9006-11 {ECO:0000313|EMBL:OBZ72095.1,
RC   ECO:0000313|Proteomes:UP000092993};
RA   Min B., Park H., Kim J.-G., Cho H., Oh Y.-L., Kong W.-S., Choi I.-G.;
RT   "Whole genome sequencing of Grifola frondosa 9006-11.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:OBZ72095.1}.
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DR   EMBL; LUGG01000009; OBZ72095.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C7M578; -.
DR   STRING; 5627.A0A1C7M578; -.
DR   OMA; VHICHRI; -.
DR   OrthoDB; 21304at2759; -.
DR   UniPathway; UPA00340; UER00458.
DR   Proteomes; UP000092993; 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; IPR023865; Aliphatic_acid_kinase_CS.
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   PRINTS; PR00471; ACETATEKNASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 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_03131};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, 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:UP000092993};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03131}.
FT   ACT_SITE        14
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT   BINDING         74..78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT   BINDING         261
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT   SITE            46
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT   SITE            107
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
SQ   SEQUENCE   279 AA;  30463 MW;  B843A5F263A59305 CRC64;
     MEALPNANSI AYFDTSFHRT IPPHISSYAI RQDIAKKRGL QKYGFHGLSY TYILHAVTVF
     LHQEPAATNL IVLHLGSGAS MCAIRAGKSL DTTMGLTPLN GLPGATRSGA VDPSLIFHYT
     NRAGRISHDR SLAVNVHVTQ AEDILNKHAG WAALTGTTDF GEIVRQMRAV EERRAAGEAV
     GEEEGKWKLA FDLFVDRVIG YVGSYFAKLG GEVDALVFSG GIGERSVELR EEVGVDGADG
     VVVDIGTSKD KKRVLVCRTD EQLEMAKECA LSEKFWRRN
//
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