ID ACKA_SHEB2 Reviewed; 399 AA.
AC B8EEJ1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 01-MAY-2013, entry version 32.
DE RecName: Full=Acetate kinase;
DE EC=2.7.2.1;
DE AltName: Full=Acetokinase;
GN Name=ackA; OrderedLocusNames=Sbal223_1691;
OS Shewanella baltica (strain OS223).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=407976;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS223;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L.,
RA Brettin T., Detter J.C., Han C., Kuske C.R., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Brettar I., Rodrigues J.,
RA Konstantinidis K., Tiedje J.;
RT "Complete sequence of chromosome of Shewanella baltica OS223.";
RL Submitted (DEC-2008) 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; CP001252; ACK46196.1; -; Genomic_DNA.
DR RefSeq; YP_002357619.1; NC_011663.1.
DR ProteinModelPortal; B8EEJ1; -.
DR STRING; 407976.Sbal223_1691; -.
DR EnsemblBacteria; ACK46196; ACK46196; Sbal223_1691.
DR GeneID; 7086297; -.
DR KEGG; sbp:Sbal223_1691; -.
DR PATRIC; 23479528; VBISheBal125792_1740.
DR eggNOG; COG0282; -.
DR HOGENOM; HOG000288398; -.
DR KO; K00925; -.
DR OMA; IDHERNL; -.
DR ProtClustDB; PRK00180; -.
DR BioCyc; SBAL407976:GJ6Y-1749-MONOMER; -.
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 1 399 Acetate kinase.
FT /FTId=PRO_1000116807.
FT NP_BIND 208 212 ATP (By similarity).
FT NP_BIND 283 285 ATP (By similarity).
FT NP_BIND 331 335 ATP (By similarity).
FT ACT_SITE 148 148 Proton donor/acceptor (By similarity).
FT METAL 10 10 Magnesium (By similarity).
FT METAL 385 385 Magnesium (By similarity).
FT BINDING 17 17 ATP (By similarity).
FT BINDING 91 91 Substrate (By similarity).
FT SITE 180 180 Transition state stabilizer (By
FT similarity).
FT SITE 241 241 Transition state stabilizer (By
FT similarity).
SQ SEQUENCE 399 AA; 43600 MW; B157D050FB9B23A4 CRC64;
MSNNLVLVLN CGSSSLKFAV IDAQTGDDQI SGLAECFGLE DSRIKWKING EKHEAALGAF
TAHREAVEYI VNKILAEQPE LAAKIQAVGH RIVHGGEKFT RSVIIDESVI KGIEDCASLA
PLHNPAHLIG IRAAIASFPK LPQVAVFDTA FHQSMPDRAY VYALPYKLYR EHGIRRYGMH
GTSHLFVSRE AAKMLNKPIE ETNVICAHLG NGASVTAIKG GKSVDTSMGL TPLEGLVMGT
RCGDIDPSII YHLVHQLGYT LEEVNNLMNK QSGLLGISEL TNDCRGIEEG YADGHKGATL
ALEIFCYRLA KYIASYTVPL GRLDAVVFTG GIGENSDLIR EKVLNMLEIF NFHVDSERNK
AARFGKKGII TQDKGTIAMV IPTNEEWVIA EDSIKLINK
//
