ID A1SKX0_NOCSJ Unreviewed; 402 AA.
AC A1SKX0;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 29-MAY-2013, entry version 55.
DE RecName: Full=Acetate kinase;
DE EC=2.7.2.1;
DE AltName: Full=Acetokinase;
GN Name=ackA; OrderedLocusNames=Noca_2953;
OS Nocardioides sp. (strain BAA-499 / JS614).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Propionibacterineae; Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=196162;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAA-499 / JS614;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Mattes T., Gossett J., Richardson P.;
RT "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL Submitted (DEC-2006) 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; CP000509; ABL82455.1; -; Genomic_DNA.
DR RefSeq; YP_924142.1; NC_008699.1.
DR ProteinModelPortal; A1SKX0; -.
DR STRING; 196162.Noca_2953; -.
DR EnsemblBacteria; ABL82455; ABL82455; Noca_2953.
DR GeneID; 4595737; -.
DR KEGG; nca:Noca_2953; -.
DR PATRIC; 22747967; VBINocSp122728_3218.
DR eggNOG; COG0282; -.
DR HOGENOM; HOG000288399; -.
DR KO; K00925; -.
DR OMA; SACAVQN; -.
DR ProtClustDB; CLSK2783633; -.
DR BioCyc; NSP196162:GH4V-2997-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:0000287; F:magnesium ion binding; IEA:HAMAP.
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 NP_BIND 211 215 ATP (By similarity).
FT NP_BIND 285 287 ATP (By similarity).
FT NP_BIND 333 337 ATP (By similarity).
FT ACT_SITE 151 151 Proton donor/acceptor (By similarity).
FT METAL 9 9 Magnesium (By similarity).
FT METAL 387 387 Magnesium (By similarity).
FT BINDING 16 16 ATP (By similarity).
FT BINDING 94 94 Substrate (By similarity).
FT SITE 183 183 Transition state stabilizer (By
FT similarity).
FT SITE 244 244 Transition state stabilizer (By
FT similarity).
SQ SEQUENCE 402 AA; 42856 MW; D0A263F9AEEA4633 CRC64;
MSALVLVINA GSSSLKYSLI DAESGASHAV GLAERIADSS GAGGSLSHTG PDGVKHRSEL
PLPSHEAALR AALDAFAAHG PSLEDATITA VGHRMVHGGE RFSEPALVDD ALVDAVRELV
PLAPLHNPAN LEALGVARRL FDTLPHVAVF DTAFHQTLPE QAYTYAVPHE WREEHGIRRY
GFHGTSHKFV SGETARLLGR PVEDTNTIVL HLGNGASATA VAGGRSVDTS MGLTPLEGLV
MGTRSGDVDP ALHAHLHRQL GWSLEEIDQR LNRNSGIKGL LGFSDFRELG RLLEEGEPRA
RLAMDVYCYR LRKYVGAYYA VLGRVDAIAF TGGVGEHVPD VRAQALAGLE RLGIRIDAEA
NRGGHSGAFT VSAEDSEVAV LVVPTNEEWQ IARESLDVVR GG
//
