ID D8I9W8_BRAP9 Unreviewed; 377 AA.
AC D8I9W8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
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 ECO:0000313|EMBL:ADK30085.1};
GN OrderedLocusNames=BP951000_0076 {ECO:0000313|EMBL:ADK30085.1};
OS Brachyspira pilosicoli (strain ATCC BAA-1826 / 95/1000).
OC Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC Brachyspira.
OX NCBI_TaxID=759914 {ECO:0000313|EMBL:ADK30085.1, ECO:0000313|Proteomes:UP000000332};
RN [1] {ECO:0000313|EMBL:ADK30085.1, ECO:0000313|Proteomes:UP000000332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1826 / 95/1000 {ECO:0000313|Proteomes:UP000000332};
RX PubMed=20625514; DOI=10.1371/journal.pone.0011455;
RA Wanchanthuek P., Bellgard M.I., La T., Ryan K., Moolhuijzen P., Chapman B.,
RA Black M., Schibeci D., Hunter A., Barrero R., Phillips N.D., Hampson D.J.;
RT "The complete genome sequence of the pathogenic intestinal spirochete
RT Brachyspira pilosicoli and comparison with other Brachyspira genomes.";
RL PLoS ONE 5:E11455-E11455(2010).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00020}.
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DR EMBL; CP002025; ADK30085.1; -; Genomic_DNA.
DR AlphaFoldDB; D8I9W8; -.
DR STRING; 759914.BP951000_0076; -.
DR KEGG; bpo:BP951000_0076; -.
DR eggNOG; COG0282; Bacteria.
DR HOGENOM; CLU_020352_0_1_12; -.
DR InParanoid; D8I9W8; -.
DR UniPathway; UPA00340; UER00458.
DR Proteomes; UP000000332; Chromosome.
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; PS01076; ACETATE_KINASE_2; 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}; Reference proteome {ECO:0000313|Proteomes:UP000000332};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00020}.
FT ACT_SITE 130
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 188..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 263..265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 310..314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 363
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT SITE 162
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT SITE 221
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
SQ SEQUENCE 377 AA; 40938 MW; 6647B783DE51528A CRC64;
MPEAKVLAKG LLEKIGEEIS ALKHTAVEKG KEKKIEQKVP DHKAGMSLIF SLLTDKEVGV
ISDMSEISGV GHRVVHGGEA FSKSTLITEE AIKAIEACCD IAPLHNPAGL QGIRACQEIL
KDVKMVAVFD TSFHQTIPEH AYMYAVPHEW YDKYKVRRYG FHGTSHKYVY GEFCKATNKP
NANVIVCHLG NGASVTAVKN GESVDTSMGL TPLEGLVMGT RSGDMDPAVV TFMMGKENLS
AKEIDNIINK KSGLLGVSGV SNDMRNLEEA SKTNPKAELA IKMFCYRVKK YIGSYMAVLG
HLDGIVFTGG IGENSAYIRG RILEGLDELG IKCDADKNAK ARGCANFEKD GAAIKLYVIA
TDEEKAIAMD TYNIALK
//
