(data stored in ACNUC29543 zone)

SWISSPROT: B2JMM7_PARP8

ID   B2JMM7_PARP8            Unreviewed;       393 AA.
AC   B2JMM7;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   08-MAY-2019, entry version 83.
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   OrderedLocusNames=Bphy_3686 {ECO:0000313|EMBL:ACC72821.1};
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC72821.1, ECO:0000313|Proteomes:UP000001192};
RN   [1] {ECO:0000313|Proteomes:UP000001192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC   {ECO:0000313|Proteomes:UP000001192};
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A.,
RA   Melkonian R., James E.K., Young J.P., Bena G., Hauser L., Land M.,
RA   Kyrpides N., Bruce D., Chain P., Copeland A., Pitluck S., Woyke T.,
RA   Lizotte-Waniewski M., Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad
RT   host range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00020}.
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DR   EMBL; CP001044; ACC72821.1; -; Genomic_DNA.
DR   RefSeq; WP_012402994.1; NC_010623.1.
DR   STRING; 391038.Bphy_3686; -.
DR   EnsemblBacteria; ACC72821; ACC72821; Bphy_3686.
DR   GeneID; 27743352; -.
DR   KEGG; bph:Bphy_3686; -.
DR   eggNOG; ENOG4105C6H; Bacteria.
DR   eggNOG; COG0282; LUCA.
DR   HOGENOM; HOG000288399; -.
DR   KO; K00925; -.
DR   OMA; FMMQKEN; -.
DR   OrthoDB; 537106at2; -.
DR   BioCyc; BPHY391038:G1GBS-3781-MONOMER; -.
DR   UniPathway; UPA00340; UER00458.
DR   Proteomes; UP000001192; Chromosome 2.
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.
PE   3: Inferred from homology;
DR   PRODOM; B2JMM7.
DR   SWISS-2DPAGE; B2JMM7.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00130545};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001192};
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:ACC72821.1};
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:UP000001192};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|RuleBase:RU003835, ECO:0000256|SAAS:SAAS00130632}.
FT   NP_BIND     208    212       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   NP_BIND     283    285       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   ACT_SITE    150    150       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   METAL         8      8       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00020}.
FT   METAL       379    379       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00020}.
FT   BINDING      15     15       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   BINDING      93     93       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00020}.
FT   SITE        181    181       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   SITE        241    241       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00020}.
SQ   SEQUENCE   393 AA;  42346 MW;  993F84A73166A9A7 CRC64;
     MDVILVINAG SSSIKFHAFH AQGAQLEPIA GGKLEEIYTN PRFTAKRQNG EVIEDKRWPE
     GEQLGHDNAI AFLLDWLRSH GEGRATLLAV GHRVVHGGDK YAEPVRVDAK VMEELEALVP
     LAPLHQPHNL AAIRSIMARN TNVPQIACFD TAFHHTQPAV ATRFALPPDI TSRGVRRYGF
     HGLSYEYIAS VLPQVDERAA KGKTVVMHLG NGASMAAFDG CKSIASTMGF TAVEGLVMGT
     RSGSLDPGVV LWMLEEANMD ARAIESLLYK RSGLLGVSGI SSDMRTLLAS DDPKAAEAVE
     LFCYRISREL GSLAAALGGL DAIVFTAGIG ERADAVRKRV GQLAAWLGVS LDEAANQRHG
     PCISDAKSAV DVWVIPTNEE LMIARHALSR LES
//

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