ID   ACKA_THELT              Reviewed;         405 AA.
AC   A8F3X9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   01-MAY-2013, entry version 39.
DE   RecName: Full=Acetate kinase;
DE            EC=2.7.2.1;
DE   AltName: Full=Acetokinase;
GN   Name=ackA; OrderedLocusNames=Tlet_0293;
OS   Thermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / TMO).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=416591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-301 / DSM 14385 / TMO;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Foster B., Bruce D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nelson K.,
RA   Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Thermotoga lettingae TMO.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate
CC       and ATP. Can also catalyze the reverse reaction (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + acetate = ADP + acetyl phosphate.
CC   -!- COFACTOR: Mg(2+). Can also accept Mn(2+) (By similarity).
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA
CC       biosynthesis; acetyl-CoA from acetate: step 1/2.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the acetokinase family.
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DR   EMBL; CP000812; ABV32863.1; -; Genomic_DNA.
DR   RefSeq; YP_001469927.1; NC_009828.1.
DR   ProteinModelPortal; A8F3X9; -.
DR   SMR; A8F3X9; 1-396.
DR   STRING; 416591.Tlet_0293; -.
DR   EnsemblBacteria; ABV32863; ABV32863; Tlet_0293.
DR   GeneID; 5608591; -.
DR   KEGG; tle:Tlet_0293; -.
DR   PATRIC; 23931083; VBITheLet125395_0312.
DR   eggNOG; COG0282; -.
DR   HOGENOM; HOG000288398; -.
DR   KO; K00925; -.
DR   OMA; LVHGGEK; -.
DR   ProtClustDB; PRK00180; -.
DR   UniPathway; UPA00340; UER00458.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008776; F:acetate kinase activity; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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/Proprionate_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;
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Transferase.
FT   CHAIN         1    405       Acetate kinase.
FT                                /FTId=PRO_1000057187.
FT   NP_BIND     207    211       ATP (By similarity).
FT   NP_BIND     282    284       ATP (By similarity).
FT   NP_BIND     330    334       ATP (By similarity).
FT   ACT_SITE    147    147       Proton donor/acceptor (By similarity).
FT   METAL         7      7       Magnesium (By similarity).
FT   METAL       383    383       Magnesium (By similarity).
FT   BINDING      14     14       ATP (By similarity).
FT   BINDING      90     90       Substrate (By similarity).
FT   SITE        179    179       Transition state stabilizer (By
FT                                similarity).
FT   SITE        240    240       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   405 AA;  45208 MW;  10876417DAE11CC4 CRC64;
     MKILVVNCGS SSVKYQFIDM KGEKVLCKGL AERVGIEGSR LVHKVNEDKH VIEKPMKDHE
     EALKLILETL LDREIGVIRD LSEISAVGHR VVHGAERFAS SILIDEEVMK VLEENIHLAP
     LHNPPNIMGI KAVQKLLPQV PNVGVFDTAF HQSMPRKAFL YPLPYEFYEK YRIRRYGFHG
     TSHRYVSKRA AEILGRDYYD FKVITCHLGN GASIAAIRHG KSIDTSMGFT PLEGLVMGTR
     SGDIDPAIVI YMQQNLSIPV EEVYNILNKK SGVLGLSKLS SDMRDIEDAA ESGNEMAQLA
     LEIYIYRIAK YIGAYTAAMN GVDAIVFTAG VGENSPYVRE KVCDYLGFLG VKIDRNLNNM
     KGVERIVSTP DSRVAILIVP TNEELVIARD TKQIVESGIK ELKLF
//