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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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