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A1B9S8 (A1B9S8_PARDP) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 57. 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

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:Pden_4208 EMBL ABL72272.1
OrganismParacoccus denitrificans (strain Pd 1222) [Complete proteome] [HAMAP] EMBL ABL72272.1
Taxonomic identifier318586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Protein attributes

Sequence length367 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. HAMAP-Rule MF_00020 RuleBase RU003835

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding203 – 2075ATP By similarity HAMAP-Rule MF_00020
Nucleotide binding323 – 3275ATP By similarity HAMAP-Rule MF_00020

Sites

Active site1451Proton donor/acceptor By similarity HAMAP-Rule MF_00020
Metal binding91Magnesium By similarity HAMAP-Rule MF_00020
Metal binding3541Magnesium By similarity HAMAP-Rule MF_00020
Binding site161ATP By similarity HAMAP-Rule MF_00020
Binding site871Substrate By similarity HAMAP-Rule MF_00020
Site1761Transition state stabilizer By similarity HAMAP-Rule MF_00020
Site2361Transition state stabilizer By similarity HAMAP-Rule MF_00020

Sequences

Sequence LengthMass (Da)Tools
A1B9S8 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: D30649F83C9EAF00

FASTA36738,600
        10         20         30         40         50         60 
MIAAILTLNA GSSSLKFRVF AREGLALLAR GAVSRIGADA ELVAELTGAS QVRSPVAGGD 

        70         80         90        100        110        120 
HAAAMQAVLD FIDAHDEGWR IEAVAHRIVH GGTRYTRSTP VTPQVLVDLA ALIPLAPLHQ 

       130        140        150        160        170        180 
PHGLAAIAAA RRLVGEDVPN LACFDTAFHA GRDALFTHFA LPEPLFEQGV RRYGFHGLSY 

       190        200        210        220        230        240 
QWLAQVLARD HPELHRGRVV AAHLGNGASL CAMHQGRSVD TTMGMTAVDG IPMGTRSGAV 

       250        260        270        280        290        300 
DPGAILLMQR SFGMTPEEIE DLIYNRSGLL GMSGRSNDVA ALLTDGSAQS RFALDFFALR 

       310        320        330        340        350        360 
CAQAAAAMAV SLGGIDAMVF TGGIGENAAP VREAILRHMA PLGDFATLVI PANEECMMAM 


EAAALLA 

« Hide

References

[1]"Complete sequence of chromosome 2 of Paracoccus denitrificans PD1222."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pd 1222.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000490 Genomic DNA. Translation: ABL72272.1.
RefSeqYP_917968.1. NC_008687.1.

3D structure databases

ProteinModelPortalA1B9S8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING318586.Pden_4208.

Proteomic databases

PRIDEA1B9S8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL72272; ABL72272; Pden_4208.
GeneID4582758.
KEGGpde:Pden_4208.
PATRIC22859604. VBIParDen97112_4155.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0282.
HOGENOMHOG000288399.
KOK00925.
OMAFHRGHPF.
OrthoDBEOG69975F.

Enzyme and pathway databases

BioCycPDEN318586:GCVQ-4250-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 nameA1B9S8_PARDP
AccessionPrimary (citable) accession number: A1B9S8
Entry history
Integrated into UniProtKB/TrEMBL: January 23, 2007
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)