Skip Header

Contribute Send feedback
Read comments (?) or add your own

F6B325 (F6B325_DESCC) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Acetate kinase HAMAP-Rule MF_00020
EC=2.7.2.1 HAMAP-Rule MF_00020
Alternative name(s):
Acetokinase HAMAP-Rule MF_00020
Gene names
Name:ackA HAMAP-Rule MF_00020
Ordered Locus Names:Desca_1059
OrganismDesulfotomaculum carboxydivorans (strain DSM 14880 / VKM B-2319 / CO-1-SRB) [Complete proteome] [HAMAP] EMBL AEF93929.1
Taxonomic identifier868595 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Peptococcaceae › Desulfotomaculum ›

Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction By similarity. HAMAP-Rule MF_00020

Catalytic activity

ATP + acetate = ADP + acetyl phosphate. HAMAP-Rule MF_00020

Cofactor

Mg2+. Can also accept Mn2+ By similarity. HAMAP-Rule MF_00020

Pathway

Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2. HAMAP-Rule MF_00020

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00020

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00020 SAAS SAAS000890.

Sequence similarities

Belongs to the acetokinase family. RuleBase RU003835

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding208 – 2125ATP By similarity HAMAP-Rule MF_00020
Nucleotide binding283 – 2853ATP By similarity HAMAP-Rule MF_00020
Nucleotide binding331 – 3355ATP By similarity HAMAP-Rule MF_00020

Sites

Active site1481Proton donor/acceptor By similarity HAMAP-Rule MF_00020
Metal binding71Magnesium By similarity HAMAP-Rule MF_00020
Metal binding3841Magnesium By similarity HAMAP-Rule MF_00020
Binding site141ATP By similarity HAMAP-Rule MF_00020
Binding site911Substrate By similarity HAMAP-Rule MF_00020
Site1801Transition state stabilizer By similarity HAMAP-Rule MF_00020
Site2411Transition state stabilizer By similarity HAMAP-Rule MF_00020

Sequences

Sequence LengthMass (Da)Tools
F6B325 [UniParc].

Last modified July 27, 2011. Version 1.
Checksum: 4818E6B65B9594CF

FASTA39843,191
        10         20         30         40         50         60 
MLILVVNCGS SSIKYKLMDM EQETVLLSGL AERIGIAGSR IKQESQAGKE LVLEQDLPNH 

        70         80         90        100        110        120 
KVALETILKC ITDQTYGAIS DISMIKAVGH RVVHGGEEFN KSVLINDELI KVLEELSDLA 

       130        140        150        160        170        180 
PLHNPPNVVG IKTCREILPG IPHVAVFDTA FHQSIPKHAF MYGIPYQYYE KYKIRKYGFH 

       190        200        210        220        230        240 
GTSHKYVSGR AAEILGKSVE ELKIIVCHLG NGSSITAVGN GVSVDTTMGF TPLAGLPMGT 

       250        260        270        280        290        300 
RTGDIDPAIV TFLMEKENLS IDETNNLLNK QSGVLGISGI SSDFRDLEDA ANQGNERAEL 

       310        320        330        340        350        360 
ALSMFAYSIN KWIGAFTAAL GGLDVVVFTG GIGENSKDMR ARVLKGLAYT GLEIDEEKNN 

       370        380        390 
SRGKEVIISK PGSPITAMVV PTNEELMIAR ETKVLATR

« Hide

References

[1]"Complete sequence of Desulfotomaculum carboxydivorans CO-1-SRB."
Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Stams A., Plugge C. expand/collapse author list , Muyzer G., Kuever J., Parshina S., Ivanova A., Nazina T., Woyke T.
Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 14880 / VKM B-2319 / CO-1-SRB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002736 Genomic DNA. Translation: AEF93929.1.
RefSeqYP_004496841.1. NC_015565.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEF93929; AEF93929; Desca_1059.
GeneID10630458.
KEGGdca:Desca_1059.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00925.

Enzyme and pathway databases

BioCycDCAR868595:GHXC-1115-MONOMER.
UniPathwayUPA00340; UER00458.

Family and domain databases

HAMAPMF_00020. Acetate_kinase.
InterProIPR004372. Ac/Proprionate_kinase.
IPR000890. Aliphatic_acid_kin_short-chain.
IPR023865. Aliphatic_acid_kinase_CS.
[Graphical view]
PANTHERPTHR21060. PTHR21060. 1 hit.
PfamPF00871. Acetate_kinase. 1 hit.
[Graphical view]
PIRSFPIRSF000722. Acetate_prop_kin. 1 hit.
PRINTSPR00471. ACETATEKNASE.
TIGRFAMsTIGR00016. ackA. 1 hit.
PROSITEPS01075. ACETATE_KINASE_1. 1 hit.
PS01076. ACETATE_KINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF6B325_DESCC
AccessionPrimary (citable) accession number: F6B325
Entry history
Integrated into UniProtKB/TrEMBL: July 27, 2011
Last sequence update: July 27, 2011
Last modified: May 29, 2013
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info