(data stored in ACNUC27125 zone)

SWISSPROT: ACKA_ACAM1

ID   ACKA_ACAM1              Reviewed;         398 AA.
AC   B0CB11;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   11-DEC-2019, entry version 67.
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}; OrderedLocusNames=AM1_0445;
OS   Acaryochloris marina (strain MBIC 11017).
OC   Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC   Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBIC 11017;
RX   PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA   Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA   Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA   Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA   Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA   Blankenship R.E., Touchman J.W.;
RT   "Niche adaptation and genome expansion in the chlorophyll d-producing
RT   cyanobacterium Acaryochloris marina.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
CC   -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate and
CC       ATP. Can also catalyze the reverse reaction. {ECO:0000255|HAMAP-
CC       Rule:MF_00020}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP = acetyl phosphate + ADP; Xref=Rhea:RHEA:11352,
CC         ChEBI:CHEBI:22191, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:456216; EC=2.7.2.1; Evidence={ECO:0000255|HAMAP-
CC         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-Rule:MF_00020};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC       acetyl-CoA from acetate: step 1/2. {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}.
DR   EMBL; CP000828; ABW25501.1; -; Genomic_DNA.
DR   RefSeq; WP_012161108.1; NC_009925.1.
DR   SMR; B0CB11; -.
DR   STRING; 329726.AM1_0445; -.
DR   EnsemblBacteria; ABW25501; ABW25501; AM1_0445.
DR   KEGG; amr:AM1_0445; -.
DR   eggNOG; ENOG4105C6H; Bacteria.
DR   eggNOG; COG0282; LUCA.
DR   HOGENOM; HOG000288398; -.
DR   KO; K00925; -.
DR   OMA; WKALTGT; -.
DR   OrthoDB; 537106at2; -.
DR   UniPathway; UPA00340; UER00458.
DR   Proteomes; UP000000268; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008776; F:acetate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
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/propionate_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;
DR   PRODOM; B0CB11.
DR   SWISS-2DPAGE; B0CB11.
KW   ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..398
FT                   /note="Acetate kinase"
FT                   /id="PRO_1000089955"
FT   NP_BIND         210..214
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   NP_BIND         284..286
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   NP_BIND         332..336
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   ACT_SITE        153
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   METAL           7
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   METAL           385
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   BINDING         14
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   BINDING         96
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   SITE            184
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   SITE            243
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
SQ   SEQUENCE   398 AA;  43410 MW;  AF3C9FEBE6DCDB4B CRC64;
     MKILVLNAGS SSHKCCLYAI EGPLPDHPAP PLWEAQLDWH DPNHASLKVK TKRENLEEDL
     SDVSRADALS HLLTTLWHGP TQVIQMAQEI NVVGHRVVHG GQDYQSSVVV TSEVKTAIAD
     LIPLAPNHNP ANLEGIKLIE QLLGNVRQVA VFDTAFHSHL PEVAAIYPGP YDWQQQGIRR
     YGFHGISHQY CTQRTAEILG RGVDRLIICH LGNGASLTAV KQGQSIDTSM GFTPLEGLMM
     GTRSGSIDPG ILIHLMRQGY DADQLDHMLN KASGLKGISG VSHDLREIEQ AIAQDNAQAK
     LARDLYLHRL KACLGSMLMS LGGVDVLVFT GGIGEHSASV RAETCEALAF LGLKLDPILN
     RKSPVDQDIA AVDSKVRVLV IKTQEDWAIA QSCYEQCC
//

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