ID A0A2G3JFL4_9NEIS Unreviewed; 397 AA.
AC A0A2G3JFL4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Acetate kinase {ECO:0000256|HAMAP-Rule:MF_00020};
DE EC=2.7.2.1 {ECO:0000256|HAMAP-Rule:MF_00020};
DE AltName: Full=Acetokinase {ECO:0000256|HAMAP-Rule:MF_00020};
GN Name=ackA {ECO:0000256|HAMAP-Rule:MF_00020};
GN ORFNames=CSQ88_02915 {ECO:0000313|EMBL:PHV03246.1};
OS Iodobacter sp. BJB302.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chitinibacteraceae; Iodobacter.
OX NCBI_TaxID=1506510 {ECO:0000313|EMBL:PHV03246.1, ECO:0000313|Proteomes:UP000224670};
RN [1] {ECO:0000313|EMBL:PHV03246.1, ECO:0000313|Proteomes:UP000224670}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BJB302 {ECO:0000313|EMBL:PHV03246.1,
RC ECO:0000313|Proteomes:UP000224670};
RA Jude B.A., Perron G.P., O'Brien K., Doing G., Bettina A.M.;
RT "Draft genomes of phenotypically distinct violacein producing isolates
RT cultured from the Hudson Valley Watershed.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate and
CC ATP. Can also catalyze the reverse reaction. {ECO:0000256|HAMAP-
CC Rule:MF_00020}.
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_00020};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00020};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00020};
CC Note=Mg(2+). Can also accept Mn(2+). {ECO:0000256|HAMAP-Rule:MF_00020};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC acetyl-CoA from acetate: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00020}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00020}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00020}.
CC -!- SIMILARITY: Belongs to the acetokinase family.
CC {ECO:0000256|ARBA:ARBA00008748, ECO:0000256|HAMAP-Rule:MF_00020,
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:PHV03246.1}.
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DR EMBL; PDZG01000005; PHV03246.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G3JFL4; -.
DR OrthoDB; 9802453at2; -.
DR UniPathway; UPA00340; UER00458.
DR Proteomes; UP000224670; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 NCBIfam; TIGR00016; ackA; 1.
DR PANTHER; PTHR21060; ACETATE KINASE; 1.
DR PANTHER; PTHR21060:SF15; PROPIONATE KINASE PDUW; 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.
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_00020};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00020};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00020};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00020};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00020};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00020};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00020}.
FT ACT_SITE 150
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 209..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 284..286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 329..333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 383
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT SITE 182
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT SITE 242
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
SQ SEQUENCE 397 AA; 42954 MW; EAF7EFE2F83EAD7A CRC64;
MSELVLVINA GSSSIKFSLF ETGAADPVLL FKGLADGIYV DPKFVAKDAD DNKLVSESMP
ADMPKNHDSA LRHMLAWLNS RIEGRTIAAV GHRVVHGGLS FCQPVRITEE VLKGLDETIA
LAPLHAPHNI MPMRVLAQLL PTVPQVACFD TAFHRTQPEI EQQYALPYEF SEKHGIRRYG
FHGLSYEYIA SVLPGIDAKA AAGRTVVAHL GNGSSMAGLI NGHCQATTMG FTALEGLPMG
TRCGTIDPAL ILHFMSHLKM DASQIEELIY KQSGLLGMSG ISSDMRDLHA SKDPHAKFAV
DYFAHRVVRE AASLAAAMQG FDALVFTAGI GENDDIARAT VCNELRWLGV EIDEVANAKR
SGEARCISLP GSRVPVYIIP TNEELMIARH ALKCVAA
//
