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Entry: ACKA_STRGG
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Original site: ACKA_STRGG 
ID   ACKA_STRGG              Reviewed;         412 AA.
AC   B1W052;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   26-NOV-2014, entry version 45.
DE   RecName: Full=Acetate kinase {ECO:0000255|HAMAP-Rule:MF_00020};
DE            EC=2.7.2.1 {ECO:0000255|HAMAP-Rule:MF_00020};
DE   AltName: Full=Acetokinase {ECO:0000255|HAMAP-Rule:MF_00020};
GN   Name=ackA {ECO:0000255|HAMAP-Rule:MF_00020};
GN   OrderedLocusNames=SGR_2112;
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=455632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350;
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism
RT   Streptomyces griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
CC   -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate
CC       and ATP. Can also catalyze the reverse reaction.
CC       {ECO:0000255|HAMAP-Rule:MF_00020}.
CC   -!- CATALYTIC ACTIVITY: ATP + acetate = ADP + acetyl phosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_00020}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00020};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00020};
CC       Note=Mg(2+). Can also accept Mn(2+). {ECO:0000255|HAMAP-
CC       Rule:MF_00020};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA
CC       biosynthesis; acetyl-CoA from acetate: step 1/2.
CC       {ECO:0000255|HAMAP-Rule:MF_00020}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00020}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00020}.
CC   -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00020}.
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DR   EMBL; AP009493; BAG18941.1; -; Genomic_DNA.
DR   RefSeq; YP_001823624.1; NC_010572.1.
DR   ProteinModelPortal; B1W052; -.
DR   SMR; B1W052; 5-401.
DR   STRING; 455632.SGR_2112; -.
DR   EnsemblBacteria; BAG18941; BAG18941; SGR_2112.
DR   GeneID; 6212001; -.
DR   KEGG; sgr:SGR_2112; -.
DR   PATRIC; 23750689; VBIStrGri32265_2144.
DR   eggNOG; COG0282; -.
DR   HOGENOM; HOG000288398; -.
DR   KO; K00925; -.
DR   OMA; MIARETV; -.
DR   OrthoDB; EOG69975F; -.
DR   BioCyc; SGRI455632:GD3A-2125-MONOMER; -.
DR   UniPathway; UPA00340; UER00458.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
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; Reference proteome; Transferase.
FT   CHAIN         1    412       Acetate kinase.
FT                                /FTId=PRO_1000089995.
FT   NP_BIND     212    216       ATP. {ECO:0000255|HAMAP-Rule:MF_00020}.
FT   NP_BIND     286    288       ATP. {ECO:0000255|HAMAP-Rule:MF_00020}.
FT   NP_BIND     334    338       ATP. {ECO:0000255|HAMAP-Rule:MF_00020}.
FT   ACT_SITE    152    152       Proton donor/acceptor.
FT                                {ECO:0000255|HAMAP-Rule:MF_00020}.
FT   METAL        10     10       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00020}.
FT   METAL       388    388       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00020}.
FT   BINDING      17     17       ATP. {ECO:0000255|HAMAP-Rule:MF_00020}.
FT   BINDING      95     95       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00020}.
FT   SITE        184    184       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00020}.
FT   SITE        245    245       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00020}.
SQ   SEQUENCE   412 AA;  43870 MW;  FE9CAB0A81943419 CRC64;
     MEPHRVLVLN SGSSSVKYQL LDMRDRSRLA SGLVERIGEE TSRLAHTPSA GGGAEPRERT
     GRIPDHDAAL KAAAEELAAD GLGLDSPELA AIGHRVVHGG LRFSAPTVIT DEVLEEIERL
     VPVAPLHNPA NITGIVTARA LRPDLPQVAV FDTAFHTTMP EAAARYAIDV ETADAHRIRR
     YGFHGTSHAY VSRKTAELLG RAPEDVNVIV LHLGNGASAS AVAGGRCVDT SMGLTPLEGL
     VMGTRSGDID PAVTFHLKRV AGMSADEIDV LLNQRSGLVG LCGDNDMRVI RRRIDEGDER
     AALAFDIYIH RLKKYIGAYT AVLGRVDAVA FTAGVGENAA PVREAAVAGL EELGMAVDAS
     LNAVRSTEPR LISPEYARVA VAVVPTDEEL EIAEQTFALV GDRGPRFGQV DN
//
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