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Database: UniProt/TrEMBL
Entry: C7NGZ7_KYTSD
LinkDB: C7NGZ7_KYTSD
Original site: C7NGZ7_KYTSD 
ID   C7NGZ7_KYTSD            Unreviewed;       395 AA.
AC   C7NGZ7;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   19-FEB-2014, entry version 39.
DE   RecName: Full=Acetate kinase;
DE            EC=2.7.2.1;
DE   AltName: Full=Acetokinase;
GN   Name=ackA; OrderedLocusNames=Ksed_11270;
OS   Kytococcus sedentarius (strain ATCC 14392 / DSM 20547 / CCM 314 / 541)
OS   (Micrococcus sedentarius).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Dermacoccaceae; Kytococcus.
OX   NCBI_TaxID=478801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14392 / DSM 20547 / CCM 314 / 541;
RX   PubMed=21304632; DOI=10.4056/sigs.761;
RA   Sims D., Brettin T., Detter J.C., Han C., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA   Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A.,
RA   Ivanova N., Mavrommatis K., Chen A., Palaniappan K., D'haeseleer P.,
RA   Chain P., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Schneider S., Goker M., Pukall R., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Kytococcus sedentarius type strain
RT   (541).";
RL   Stand. Genomic Sci. 1:12-20(2009).
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; CP001686; ACV06167.1; -; Genomic_DNA.
DR   RefSeq; YP_003148932.1; NC_013169.1.
DR   ProteinModelPortal; C7NGZ7; -.
DR   STRING; 478801.Ksed_11270; -.
DR   EnsemblBacteria; ACV06167; ACV06167; Ksed_11270.
DR   GeneID; 8372635; -.
DR   KEGG; kse:Ksed_11270; -.
DR   PATRIC; 22191911; VBIKytSed14067_1071.
DR   eggNOG; COG0282; -.
DR   HOGENOM; HOG000288399; -.
DR   KO; K00925; -.
DR   OMA; FVIKTNE; -.
DR   OrthoDB; EOG69975F; -.
DR   BioCyc; KSED478801:GI4L-1122-MONOMER; -.
DR   UniPathway; UPA00340; UER00458.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008776; F:acetate kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-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     203    207       ATP (By similarity).
FT   NP_BIND     276    278       ATP (By similarity).
FT   NP_BIND     324    328       ATP (By similarity).
FT   ACT_SITE    143    143       Proton donor/acceptor (By similarity).
FT   METAL         7      7       Magnesium (By similarity).
FT   METAL       381    381       Magnesium (By similarity).
FT   BINDING      14     14       ATP (By similarity).
FT   BINDING      86     86       Substrate (By similarity).
FT   SITE        175    175       Transition state stabilizer (By
FT                                similarity).
FT   SITE        236    236       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   395 AA;  41677 MW;  89DC9CB061394242 CRC64;
     MSALVINAGS SSVKFQVVDP ATGAVRAKGL AERIGETEGA ATIEQEGQGE QSTSQPFADH
     RAALAWVLDQ LGGAGLLADV EVVGHRTVHG GRRFDRPVVL DDETLAVLRE LSPLAPLHNP
     ANIEGIEAAR EQLPEVPHVS VFDTGFFAEL PPEVRTYAID TEVAQEYAVQ RYGFHGASHA
     YVSQRAAEDL GRDPAELKVI VLHLGNGASA AAVDGGRPVD CSMGMTPLEG LVMGTRPGDI
     DPGVLLHLLR HGLDADELDD LLNRRSGLKG LTGTNDMREV RAAATAGDER ARLALDVSIH
     RIVRYVGAFH AVMGGLDALV FTAGVGENNV ELRAEVCERL AVLGIRLDAG RNTSVPRGRP
     GSTVVSGDDS QVAVLVTPTN EELYIARAAA ATVTP
//
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