(data stored in SCRATCH zone)

SWISSPROT: ACKA_LACP3

ID   ACKA_LACP3              Reviewed;         396 AA.
AC   Q03CP2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   11-DEC-2019, entry version 76.
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}; OrderedLocusNames=LSEI_0166;
OS   Lactobacillus paracasei (strain ATCC 334 / BCRC 17002 / CIP 107868 / KCTC
OS   3260 / NRRL B-441).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=321967;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 334 / BCRC 17002 / CIP 107868 / KCTC 3260 / NRRL B-441;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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}.
DR   EMBL; CP000423; ABJ69030.1; -; Genomic_DNA.
DR   RefSeq; WP_003562823.1; NC_008526.1.
DR   RefSeq; YP_805472.1; NC_008526.1.
DR   SMR; Q03CP2; -.
DR   EnsemblBacteria; ABJ69030; ABJ69030; LSEI_0166.
DR   GeneID; 4419118; -.
DR   KEGG; lca:LSEI_0166; -.
DR   PATRIC; fig|321967.11.peg.191; -.
DR   HOGENOM; HOG000288398; -.
DR   KO; K00925; -.
DR   OMA; CHLGGSS; -.
DR   UniPathway; UPA00340; UER00458.
DR   Proteomes; UP000001651; 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   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   PANTHER; PTHR21060; PTHR21060; 1.
DR   Pfam; PF00871; Acetate_kinase; 1.
DR   PIRSF; PIRSF000722; Acetate_prop_kin; 1.
DR   PRINTS; PR00471; ACETATEKNASE.
DR   TIGRFAMs; TIGR00016; ackA; 1.
DR   PROSITE; PS01075; ACETATE_KINASE_1; 1.
DR   PROSITE; PS01076; ACETATE_KINASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q03CP2.
DR   SWISS-2DPAGE; Q03CP2.
KW   ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..396
FT                   /note="Acetate kinase"
FT                   /id="PRO_1000002238"
FT   NP_BIND         207..211
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   NP_BIND         283..285
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   NP_BIND         330..334
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   ACT_SITE        147
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   METAL           8
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   METAL           384
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   BINDING         15
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   BINDING         90
FT                   /note="Substrate"
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   SITE            240
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
SQ   SEQUENCE   396 AA;  43261 MW;  6131C9E55E5EE8FB CRC64;
     MAKILAVNAG SSTLKWKLFD MPAEVQLAEG LVDRLGQPQS KVKIKYGDGQ KYESDTPIAN
     YQEAVASLMG NIKALGLVEH LHEITGVGHR VVAGGETFAE SVVVDDATLL QIQNLRDYAP
     LHNPVEADYI DVFKKMMPWA TEVAVFDTAF HQTMQPENFL YSIPYDYYKK YGARKYGAHG
     TSVRYVSARA AEMLNKPLED LRMIVMHLGS GSSVTAVQGG QSIDTSMGFT PLAGVTMGTR
     SGDIDPSLVA YLMKKLDVPD VGQMIHILNN DSGLLGISGI SNDMRDLEAD EDTKPRAKLA
     LDIFVNRVVK YVGSYAALMD GVDVLVFTAG IGENGDEIRD KIMRSLDYLG AKIDNDINYK
     SHGVEADLST PDSTVKTLLV PTNEELMIVR DVMALS
//

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