ACKA1_LACLA
ID ACKA1_LACLA Reviewed; 395 AA.
AC Q9CE35;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Acetate kinase 1 {ECO:0000255|HAMAP-Rule:MF_00020};
DE EC=2.7.2.1 {ECO:0000255|HAMAP-Rule:MF_00020};
DE AltName: Full=Acetokinase 1 {ECO:0000255|HAMAP-Rule:MF_00020};
GN Name=ackA1 {ECO:0000255|HAMAP-Rule:MF_00020}; OrderedLocusNames=LL2013;
GN ORFNames=L73818;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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; AE005176; AAK06111.1; -; Genomic_DNA.
DR PIR; E86876; E86876.
DR RefSeq; NP_268170.1; NC_002662.1.
DR RefSeq; WP_004254593.1; NC_002662.1.
DR AlphaFoldDB; Q9CE35; -.
DR SMR; Q9CE35; -.
DR STRING; 272623.L73818; -.
DR PaxDb; Q9CE35; -.
DR EnsemblBacteria; AAK06111; AAK06111; L73818.
DR KEGG; lla:L73818; -.
DR PATRIC; fig|272623.7.peg.2168; -.
DR eggNOG; COG0282; Bacteria.
DR HOGENOM; CLU_020352_0_1_9; -.
DR OMA; KIITCHI; -.
DR UniPathway; UPA00340; UER00458.
DR Proteomes; UP000002196; 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 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.
DR PROSITE; PS01076; ACETATE_KINASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..395
FT /note="Acetate kinase 1"
FT /id="PRO_0000107569"
FT ACT_SITE 146
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 89
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 283..285
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 330..334
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 382
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT SITE 178
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT SITE 239
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
SQ SEQUENCE 395 AA; 43138 MW; 27D3C29227FA5724 CRC64;
MTKTLAVNAG SSSMKWQMYE MPEEKVLAKG LIERIGLKDS IVTVKFGEQK EERVFDIPNH
TEAVEVLLED LKRLKIVEEF TEITGVGHRV VAGGEIFQKS TVVTPEVLQQ VKDLSALAPL
HNPANAAGIE AFLNLLPDAT SVVVFDTAFH TTMPEKAFRY PLPKKYYTDY AVRKYGAHGT
SHMYVSQEAA KLLGKPIEET KIITAHIGNG ASLTAVKGGK SIDTSMGFTP LAGVMMGTRT
GEMDPSVFPY LIENDSELKD AQGVVDMMNK ESGLYGVSGI SSDMRDIIAA KDTDTDAKLA
FEMYVDRIQK FIGQYLAVLN GADALVFTAG IGENSVPVRE AILSGLTWFG IEVDPEKNVF
GVEGEISTPH SRVKVFVIPT DEELVIARDV EALKK
