ID Q2YAC6_NITMU Unreviewed; 376 AA.
AC Q2YAC6;
DT 20-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 127.
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 OrderedLocusNames=Nmul_A0992 {ECO:0000313|EMBL:ABB74295.1};
GN ORFNames=SAMN05216403_102168 {ECO:0000313|EMBL:SEF49724.1};
OS Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=323848 {ECO:0000313|EMBL:ABB74295.1, ECO:0000313|Proteomes:UP000002718};
RN [1] {ECO:0000313|Proteomes:UP000002718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25196 / NCIMB 11849 / C 71
RC {ECO:0000313|Proteomes:UP000002718};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT 25196.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABB74295.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 25196 {ECO:0000313|EMBL:ABB74295.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Richardson P.;
RT "Complete sequence of Chromosome 1 of Nitrosospira multiformis ATCC
RT 25196.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ABB74295.1, ECO:0000313|Proteomes:UP000002718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25196 {ECO:0000313|EMBL:ABB74295.1}, and ATCC 25196 /
RC NCIMB 11849 / C 71 {ECO:0000313|Proteomes:UP000002718};
RX PubMed=18390676; DOI=10.1128/AEM.02722-07;
RA Norton J.M., Klotz M.G., Stein L.Y., Arp D.J., Bottomley P.J., Chain P.S.,
RA Hauser L.J., Land M.L., Larimer F.W., Shin M.W., Starkenburg S.R.;
RT "Complete genome sequence of Nitrosospira multiformis, an ammonia-oxidizing
RT bacterium from the soil environment.";
RL Appl. Environ. Microbiol. 74:3559-3572(2008).
RN [4] {ECO:0000313|EMBL:SEF49724.1, ECO:0000313|Proteomes:UP000236751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nl13 {ECO:0000313|EMBL:SEF49724.1,
RC ECO:0000313|Proteomes:UP000236751};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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. {ECO:0000256|HAMAP-
CC Rule:MF_00020, ECO:0000256|RuleBase:RU003835}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00020}.
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DR EMBL; CP000103; ABB74295.1; -; Genomic_DNA.
DR EMBL; FNVK01000002; SEF49724.1; -; Genomic_DNA.
DR RefSeq; WP_011380340.1; NC_007614.1.
DR AlphaFoldDB; Q2YAC6; -.
DR STRING; 323848.Nmul_A0992; -.
DR KEGG; nmu:Nmul_A0992; -.
DR eggNOG; COG0282; Bacteria.
DR HOGENOM; CLU_020352_0_0_4; -.
DR UniPathway; UPA00340; UER00458.
DR Proteomes; UP000002718; Chromosome.
DR Proteomes; UP000236751; 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; 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; 2.
DR PRINTS; PR00471; ACETATEKNASE.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00020};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00020};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00020, ECO:0000256|RuleBase:RU003835};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00020};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00020};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00020};
KW Reference proteome {ECO:0000313|Proteomes:UP000002718};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00020,
KW ECO:0000256|RuleBase:RU003835}.
FT ACT_SITE 127
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 262..264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 307..311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT SITE 159
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT SITE 220
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
SQ SEQUENCE 376 AA; 40980 MW; B872E01A115176AD CRC64;
MRSAQALAMK ILTVNTGSSS VRLAAFLHHQ EKLTELVSVR EDSGGEPEDI LQEFVQVHKL
GKVNVVAHRV VHGGMRLTSP CVIDRDVERE IECLAPLAPL HNPVALEWIR AAKEVFGIHM
PQVAVFDTAF FTHLPTVAQT YAIPHELTGK YALRRYGFHG LAHQAMWQAW RDQHPDFVQN
GKIISMQFGA GCSITATEKG LPRDTSMGFS PLEGLMMATR SGDLDPGLMT FLQRQESLAP
EQMDRLLNEQ SGLSGVSGIS ADIRELLKSK DEYAGLAVEL YCYRARKYLG AYLAVLGGAN
AVIFGGGVGE NVPVVREKIL AGMEWCGIHL DAKKNSDASG MSCISSEASR VEVWVAPVNE
ATILAQEAEA VISSRG
//
