GenomeNet

Database: UniProt/SWISS-PROT
Entry: ACKA_STRAW
LinkDB: ACKA_STRAW
Original site: ACKA_STRAW 
ID   ACKA_STRAW              Reviewed;         405 AA.
AC   Q82JD1;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   01-OCT-2014, entry version 74.
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=SAV_2824;
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 /
OS   NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=227882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 /
RC   MA-4680;
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C.,
RA   Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T.,
RA   Kikuchi H., Shiba T., Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces
RT   avermitilis: deducing the ability of producing secondary
RT   metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 /
RC   MA-4680;
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(2003).
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: 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BA000030; BAC70535.1; -; Genomic_DNA.
DR   RefSeq; NP_824000.1; NC_003155.4.
DR   ProteinModelPortal; Q82JD1; -.
DR   STRING; 227882.SAV_2824; -.
DR   EnsemblBacteria; BAC70535; BAC70535; SAV_2824.
DR   GeneID; 1210559; -.
DR   KEGG; sma:SAV_2824; -.
DR   PATRIC; 23719229; VBIStrAve112782_3024.
DR   eggNOG; COG0282; -.
DR   HOGENOM; HOG000288399; -.
DR   KO; K00925; -.
DR   OMA; WANEVAV; -.
DR   OrthoDB; EOG69975F; -.
DR   BioCyc; SAVE227882:GJU1-2845-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; Reference proteome; Transferase.
FT   CHAIN         1    405       Acetate kinase.
FT                                /FTId=PRO_0000107620.
FT   NP_BIND     210    214       ATP. {ECO:0000255|HAMAP-Rule:MF_00020}.
FT   NP_BIND     284    286       ATP. {ECO:0000255|HAMAP-Rule:MF_00020}.
FT   NP_BIND     332    336       ATP. {ECO:0000255|HAMAP-Rule:MF_00020}.
FT   ACT_SITE    150    150       Proton donor/acceptor.
FT                                {ECO:0000255|HAMAP-Rule:MF_00020}.
FT   METAL        10     10       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00020}.
FT   METAL       386    386       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00020}.
FT   BINDING      17     17       ATP. {ECO:0000255|HAMAP-Rule:MF_00020}.
FT   BINDING      93     93       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00020}.
FT   SITE        182    182       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00020}.
FT   SITE        243    243       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00020}.
SQ   SEQUENCE   405 AA;  43242 MW;  E832A7531B3750EA CRC64;
     MSPTRVLVLN SGSSSVKYQL LDMRDSSRLA VGLVERIGEG TSRLKHTPLT TGVSRELTSP
     VADHAAALKT VAEELAKDGL GLDSPELAAI GHRVVHGGRS FTEPTVIDDD VLAEIERLIP
     VAPLHNPANL TGIRTAMALR PDLPQVAVFD TAFHTTMPES AARYAIDVKT ADEHRVRRYG
     FHGTSHAYVS RATAKLLGRA PKDVNLIVLH LGNGASASAV RGGRCVDTSM GLTPLEGLVM
     GTRSGDMDPA VIFHLMRVGG MSTDEVDTLL NTKSGLIGLC GDNDMREIRR RVDEGDEQAA
     LAFDIYIHRL KKYIGAYYAV LGRVDAVAFT AGVGENAAPV RAAAIAGLEE LGLVVDSERN
     AVRSDEPRIV SPEDARVAVA VVPTDEELEI AQQTYALVGT AHHLT
//
DBGET integrated database retrieval system