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Entry: ACKA_CORA7
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Original site: ACKA_CORA7 
ID   ACKA_CORA7              Reviewed;         406 AA.
AC   C3PJJ2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   01-OCT-2014, entry version 36.
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=cauri_2287;
OS   Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CN-1)
OS   (Corynebacterium nigricans).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=548476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700975 / DSM 44827 / CN-1;
RX   PubMed=20137072; DOI=10.1186/1471-2164-11-91;
RA   Trost E., Gotker S., Schneider J., Schneiker-Bekel S.,
RA   Szczepanowski R., Tilker A., Viehoever P., Arnold W., Bekel T.,
RA   Blom J., Gartemann K.H., Linke B., Goesmann A., Puhler A.,
RA   Shukla S.K., Tauch A.;
RT   "Complete genome sequence and lifestyle of black-pigmented
RT   Corynebacterium aurimucosum ATCC 700975 (formerly C. nigricans CN-1)
RT   isolated from a vaginal swab of a woman with spontaneous abortion.";
RL   BMC Genomics 11:91-91(2010).
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}.
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DR   EMBL; CP001601; ACP33878.1; -; Genomic_DNA.
DR   RefSeq; YP_002835816.1; NC_012590.1.
DR   ProteinModelPortal; C3PJJ2; -.
DR   STRING; 169292.cauri_2287; -.
DR   EnsemblBacteria; ACP33878; ACP33878; cauri_2287.
DR   GeneID; 7801420; -.
DR   KEGG; car:cauri_2287; -.
DR   PATRIC; 21480640; VBICorAur68407_2318.
DR   eggNOG; COG0282; -.
DR   HOGENOM; HOG000288398; -.
DR   KO; K00925; -.
DR   OMA; WANEVAV; -.
DR   OrthoDB; EOG69975F; -.
DR   BioCyc; CAUR548476:GH9E-2346-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    406       Acetate kinase.
FT                                /FTId=PRO_1000116798.
FT   NP_BIND     209    213       ATP. {ECO:0000255|HAMAP-Rule:MF_00020}.
FT   NP_BIND     283    285       ATP. {ECO:0000255|HAMAP-Rule:MF_00020}.
FT   NP_BIND     331    335       ATP. {ECO:0000255|HAMAP-Rule:MF_00020}.
FT   ACT_SITE    149    149       Proton donor/acceptor.
FT                                {ECO:0000255|HAMAP-Rule:MF_00020}.
FT   METAL         8      8       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00020}.
FT   METAL       385    385       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00020}.
FT   BINDING      15     15       ATP. {ECO:0000255|HAMAP-Rule:MF_00020}.
FT   BINDING      92     92       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00020}.
FT   SITE        181    181       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00020}.
FT   SITE        242    242       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00020}.
SQ   SEQUENCE   406 AA;  44267 MW;  589D564236E71337 CRC64;
     MAYVLVLNSG SSSVKFQLVD PESSATDTPL VSGLVEQVGE PQGAVTVKTG GEEFKEELEI
     PTHSFGLDRA FSIMHEHGVG PTDVEVIAVG HRVVHGGRLF SEPQLIVDQI ESMIEDLIPL
     APLHNPANLD GIRVARKLLP EIPHVAVFDT AFFNHMPPAA ALYAINNDVA SQYDIRRYGF
     HGTSHEFVSQ QVPKLLDRDP GHVHQITLHL GNGASAAAIR NGRPIDTSMG LTPLAGLAMG
     TRSGDIDPGI IFHLSREAGM SIDEIDNLLN KRSGVKGIAG VNDFRVLRER INNEDQDAWL
     AYNIYIHQLR RFIGAYMIAL GRVDAITFTA GVGENDTEVR QDSLYNLDMY GIDFDKEANL
     VRSKEPRMIS TADSQVKVFV VPTNEELAIA QKSAGIAAMA REAGLY
//
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