ACKA_RHIML
ID ACKA_RHIML Reviewed; 393 AA.
AC Q9X449; Q9XDG2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Acetate kinase {ECO:0000255|HAMAP-Rule:MF_00020};
DE EC=2.7.2.1 {ECO:0000255|HAMAP-Rule:MF_00020};
DE AltName: Full=Acetokinase {ECO:0000255|HAMAP-Rule:MF_00020};
GN Name=ackA {ECO:0000255|HAMAP-Rule:MF_00020};
OS Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=382;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=104A14;
RX PubMed=10094701; DOI=10.1128/jb.181.7.2217-2224.1999;
RA Summers M.L., Denton M.C., McDermott T.R.;
RT "Genes coding for phosphotransacetylase and acetate kinase in Sinorhizobium
RT meliloti are in an operon that is inducible by phosphate stress and
RT controlled by phoB.";
RL J. Bacteriol. 181:2217-2224(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 207-314.
RC STRAIN=104A14;
RX PubMed=9805396; DOI=10.1094/mpmi.1998.11.11.1094;
RA Summers M.L., Elkins J.G., Elliott B.A., McDermott T.R.;
RT "Expression and regulation of phosphate stress inducible genes in
RT Sinorhizobium meliloti.";
RL Mol. Plant Microbe Interact. 11:1094-1101(1998).
CC -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate and
CC ATP. Can also catalyze the reverse reaction. {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_00020};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00020};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00020};
CC Note=Mg(2+). Can also accept Mn(2+). {ECO:0000255|HAMAP-Rule:MF_00020};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC acetyl-CoA from acetate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00020}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00020}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00020}.
CC -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00020}.
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DR EMBL; AF095903; AAD24358.1; -; Genomic_DNA.
DR EMBL; AF074452; AAD42996.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9X449; -.
DR SMR; Q9X449; -.
DR UniPathway; UPA00340; UER00458.
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 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; PTHR21060; 1.
DR Pfam; PF00871; Acetate_kinase; 1.
DR PIRSF; PIRSF000722; Acetate_prop_kin; 1.
DR PRINTS; PR00471; ACETATEKNASE.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00016; ackA; 1.
DR PROSITE; PS01075; ACETATE_KINASE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..393
FT /note="Acetate kinase"
FT /id="PRO_0000107604"
FT ACT_SITE 148
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 206..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 280..282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 325..329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 376
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT SITE 179
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT CONFLICT 209..212
FT /note="SGAS -> AEFR (in Ref. 2; AAD42996)"
FT /evidence="ECO:0000305"
FT CONFLICT 227..238
FT /note="LHRPSTGCRWDT -> GFTALDGLPMGTR (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 42135 MW; 48FD185524CD6D4C CRC64;
MDALLVVNAG SSSLKFQVFG IVGMDLTRQI RGKVDGIGTR PRLQATAADG TQLIDQTYDA
KAVRDLPAAI TEARRWLLTL EGFELQAVGH RVVHGGPDYT RPVLIDATVL DHLAGYQDLA
PLHQPNNLAP IRLAMEINPD VPQVACFDTA FHRGHAKHTD CYALPRSFYD EGVRRYGFHG
LSYEYIAERL REVASRAAKG RVVVAHLGSG ASMCGLRDGR SIESTMLHRP STGCRWDTPG
QLDPGVVLYL ILQKGMKAQA VSDLLYHDAG LKGLSGLSND MRDLLASDDP HAALSVAHFV
YRCVLNGGML AAALGGIDAF VFTAGVGENS PPIRARIVEG LAWLGAELDP AANEAGAALI
STATSRVAVH VLPTDEELMI ARHTLALISA PNA
