(data stored in ACNUC9435 zone)

SWISSPROT: ACKA2_LISIN

ID   ACKA2_LISIN             Reviewed;         397 AA.
AC   Q92CN9;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   11-DEC-2019, entry version 98.
DE   RecName: Full=Acetate kinase 2 {ECO:0000255|HAMAP-Rule:MF_00020};
DE            EC=2.7.2.1 {ECO:0000255|HAMAP-Rule:MF_00020};
DE   AltName: Full=Acetokinase 2 {ECO:0000255|HAMAP-Rule:MF_00020};
GN   Name=ackA2 {ECO:0000255|HAMAP-Rule:MF_00020}; OrderedLocusNames=lin1132;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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; AL596167; CAC96363.1; -; Genomic_DNA.
DR   PIR; AC1574; AC1574.
DR   RefSeq; WP_010990790.1; NC_003212.1.
DR   SMR; Q92CN9; -.
DR   STRING; 272626.lin1132; -.
DR   EnsemblBacteria; CAC96363; CAC96363; CAC96363.
DR   KEGG; lin:AckA2; -.
DR   eggNOG; ENOG4105C6H; Bacteria.
DR   eggNOG; COG0282; LUCA.
DR   HOGENOM; HOG000288398; -.
DR   KO; K00925; -.
DR   OMA; IHYLYSI; -.
DR   OrthoDB; 537106at2; -.
DR   BioCyc; GCF_000195795:LIN_RS05770-MONOMER; -.
DR   UniPathway; UPA00340; UER00458.
DR   Proteomes; UP000002513; 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; Q92CN9.
DR   SWISS-2DPAGE; Q92CN9.
KW   ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..397
FT                   /note="Acetate kinase 2"
FT                   /id="PRO_0000107576"
FT   NP_BIND         206..210
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   NP_BIND         281..283
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   NP_BIND         329..333
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   ACT_SITE        146
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   METAL           8
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   METAL           380
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   BINDING         15
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   BINDING         89
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   SITE            178
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT   SITE            239
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
SQ   SEQUENCE   397 AA;  43115 MW;  5822544EF92CBF51 CRC64;
     MHKIMAINAG SSSLKFQIFT MPGEEVLVKG LIERIGLPDA IFNMSFQNEK IKETRAINNH
     GEAVEILLEQ LKTHQVINDL NEITGVGHRV AHGGEAFVSS CIVTDDVVKG IEDVTSLAPL
     HNPANIIGIK TFRELLPNAV SVAVFDTAFH QTIPEENFLY ALPYELYEKH HIRKYGFHGT
     SHKYVAGKAA EVLKKPLEKL KIISCHLGNG ASVCAIEAGK SVNTSMGFTP NAGLMMGTRS
     GTIDATIIPY LVDELGYSLD EVTHMMSSES GVLGVSGISS DFRDIEIAAN EGNSRALLTL
     RMFTGQICNY IGAYASAMNG CDALLFTAGV GENSPLIRKM VTEQLSYLGV TCNVTKNNAG
     DMIISNDDEA VKVCIIPTNE ELMIARDVEK YTKQTIS
//

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