(data stored in SCRATCH zone)

SWISSPROT: Q13IW1_PARXL

ID   Q13IW1_PARXL            Unreviewed;       397 AA.
AC   Q13IW1;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 98.
DE   RecName: Full=Acetate kinase {ECO:0000256|HAMAP-Rule:MF_00020};
DE            EC=2.7.2.1 {ECO:0000256|HAMAP-Rule:MF_00020};
DE   AltName: Full=Acetokinase {ECO:0000256|HAMAP-Rule:MF_00020};
GN   Name=ackA {ECO:0000256|HAMAP-Rule:MF_00020};
GN   ORFNames=Bxe_C0051 {ECO:0000313|EMBL:ABE35978.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE35978.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE35978.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE35978.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate
CC       and ATP. Can also catalyze the reverse reaction.
CC       {ECO:0000256|HAMAP-Rule:MF_00020}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP = acetyl phosphate + ADP;
CC         Xref=Rhea:RHEA:11352, ChEBI:CHEBI:22191, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.2.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00020};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00020};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00020};
CC       Note=Mg(2+). Can also accept Mn(2+). {ECO:0000256|HAMAP-
CC       Rule:MF_00020};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA
CC       biosynthesis; acetyl-CoA from acetate: step 1/2.
CC       {ECO:0000256|HAMAP-Rule:MF_00020}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00020}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00020,
CC       ECO:0000256|SAAS:SAAS00011667}.
CC   -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00020, ECO:0000256|RuleBase:RU003835,
CC       ECO:0000256|SAAS:SAAS00688878}.
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DR   EMBL; CP000272; ABE35978.1; -; Genomic_DNA.
DR   RefSeq; WP_011493238.1; NZ_CP008761.1.
DR   STRING; 266265.Bxe_C0051; -.
DR   EnsemblBacteria; ABE35978; ABE35978; Bxe_C0051.
DR   GeneID; 4009598; -.
DR   KEGG; bxb:DR64_8373; -.
DR   KEGG; bxe:Bxe_C0051; -.
DR   PATRIC; fig|266265.5.peg.7831; -.
DR   eggNOG; ENOG4105C6H; Bacteria.
DR   eggNOG; COG0282; LUCA.
DR   HOGENOM; HOG000288399; -.
DR   KO; K00925; -.
DR   OMA; PLPWRYY; -.
DR   OrthoDB; 537106at2; -.
DR   BioCyc; BXEN266265:BXE_RS37010-MONOMER; -.
DR   UniPathway; UPA00340; UER00458.
DR   Proteomes; UP000001817; Chromosome 3.
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; PS01076; ACETATE_KINASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13IW1.
DR   SWISS-2DPAGE; Q13IW1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00130545};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00011637};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|RuleBase:RU003835, ECO:0000256|SAAS:SAAS00130569,
KW   ECO:0000313|EMBL:ABE35978.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00011608};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00011656};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00130625};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|RuleBase:RU003835, ECO:0000256|SAAS:SAAS00130632,
KW   ECO:0000313|EMBL:ABE35978.1}.
FT   NP_BIND     207    211       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   NP_BIND     282    284       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   NP_BIND     327    331       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   ACT_SITE    149    149       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   METAL        10     10       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00020}.
FT   METAL       378    378       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00020}.
FT   BINDING      17     17       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   BINDING      92     92       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00020}.
FT   SITE        180    180       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   SITE        240    240       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00020}.
SQ   SEQUENCE   397 AA;  42030 MW;  D4A581FE8A3C4388 CRC64;
     MNDPLLLTFN PGSSTVKIGL FSVSAERATR IGQGSIDFRH APLSLHLVDG GGTREIALKA
     VVTEHLHEVL DETLNWFATH FSLTDLVSVG HRVVHGGDRF AGPAEITDAT LASIVELVPL
     APLHQPQSVR LIRAIRHLRP NLAQSASFDT AFHRTQTELV RRFALPRHFF DSGVKRYGFH
     GLSYRFIAGA LTRRFPLLAH SKVIAAHLGS GASLCAMSAG ASRDTSMGFS TLDGIPMATR
     CGALDAGVVL HLLGQPGMTP DALEKILYEQ SGLLGVSGIS ADSRELAAST QPQAQEALDL
     FVLRIAGEAA RLATTLGGLD CLVFTAGIGE HQPPIRAAVC KALAWLGVEL DDAANARNAA
     VISSSASRVA VLVIATDEEQ VIADETVSIL HSQGATA
//

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