ID   F2GMC6_MYCTU            Unreviewed;       385 AA.
AC   F2GMC6;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   01-MAY-2013, entry version 17.
DE   RecName: Full=Acetate kinase;
DE            EC=2.7.2.1;
DE   AltName: Full=Acetokinase;
GN   Name=ackA; ORFNames=TBSG_00413;
OS   Mycobacterium tuberculosis KZN 4207.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=478433;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KZN 4207;
RG   The Broad Institute Genome Sequencing Platform, Broad Institute
RG   Microbial Sequencing Center.;
RA   Murray M., Pillay M., Borowsky M.L., Young S.K., Kodira C., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chen Z.,
RA   Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.D.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J.,
RA   Yandava C., Nusbaum C., Galagan J., Birren B.;
RT   "The Genome Sequence of Mycobacterium tuberculosis strain KZN 4207.";
RL   Submitted (JUL-2009) 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; CP001662; AEB02542.1; -; Genomic_DNA.
DR   RefSeq; YP_005098881.1; NC_016768.1.
DR   ProteinModelPortal; F2GMC6; -.
DR   SMR; F2GMC6; 5-382.
DR   EnsemblBacteria; AEB02542; AEB02542; TBSG_00413.
DR   GeneID; 11694297; -.
DR   KEGG; mtk:TBSG_00413; -.
DR   KO; K00925; -.
DR   OMA; ERNNIRA; -.
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: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; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Transferase.
FT   NP_BIND     192    196       ATP (By similarity).
FT   NP_BIND     266    268       ATP (By similarity).
FT   NP_BIND     314    318       ATP (By similarity).
FT   ACT_SITE    132    132       Proton donor/acceptor (By similarity).
FT   METAL         9      9       Magnesium (By similarity).
FT   METAL       368    368       Magnesium (By similarity).
FT   BINDING      16     16       ATP (By similarity).
FT   BINDING      75     75       Substrate (By similarity).
FT   SITE        164    164       Transition state stabilizer (By
FT                                similarity).
FT   SITE        225    225       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   385 AA;  41318 MW;  AE1F50C1665B4A4C CRC64;
     MSSTVLVINS GSSSLKFQLV EPVAGMSRAA GIVERIGERS SPVADHAQAL HRAFKMLAED
     GIDLQTCGLV AVGHRVVHGG TEFHQPTLLD DTVIGKLEEL SALAPLHNPP AVLGIKVARR
     LLANVAHVAV FDTAFFHDLP PAAATYAIDR DVADRWHIRR YGFHGTSHQY VSERAAAFLG
     RPLDGLNQIV LHLGNGASAS AIARGRPVET SMGLTPLEGL VMGTRSGDLD PGVISYLWRT
     ARMGVEDIES MLNHRSGMLG LAGERDFRRL RLVIETGDRS AQLAYEVFIH RLRKYLGAYL
     AVLGHTDVVS FTAGIGENDA AVRRDALAGL QGLGIALDQD RNLGPGHGAR RISSDDSPIA
     VLVVPTNEEL AIARDCLRVL GGRRA
//