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D5T4Q4 (D5T4Q4_LEUKI) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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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:LKI_09930 EMBL ADG41525.1
OrganismLeuconostoc kimchii (strain IMSNU 11154 / KCTC 2386 / IH25) [Complete proteome] [HAMAP] EMBL ADG41525.1
Taxonomic identifier762051 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Leuconostocaceae › Leuconostoc ›

Protein attributes

Sequence length415 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 binding228 – 2325ATP By similarity HAMAP-Rule MF_00020
Nucleotide binding303 – 3053ATP By similarity HAMAP-Rule MF_00020
Nucleotide binding350 – 3545ATP By similarity HAMAP-Rule MF_00020

Sites

Active site1681Proton donor/acceptor By similarity HAMAP-Rule MF_00020
Metal binding81Magnesium By similarity HAMAP-Rule MF_00020
Metal binding4031Magnesium By similarity HAMAP-Rule MF_00020
Binding site151ATP By similarity HAMAP-Rule MF_00020
Binding site1111Substrate By similarity HAMAP-Rule MF_00020
Site2001Transition state stabilizer By similarity HAMAP-Rule MF_00020
Site2611Transition state stabilizer By similarity HAMAP-Rule MF_00020

Sequences

Sequence LengthMass (Da)Tools
D5T4Q4 [UniParc].

Last modified July 13, 2010. Version 1.
Checksum: 2145BD86E9B13334

FASTA41545,734
        10         20         30         40         50         60 
MSKIMAVNAG SSSLKFQLLE MPEEMVLMQG IIERIGQDNA EISIKYGKDI EPKRLIGAEE 

        70         80         90        100        110        120 
GHITLTKNGG QKFEHEMAIK DHDQAIDVLL QKLTDLGIVK DFNEITGVGH RVVAGGEWFN 

       130        140        150        160        170        180 
HSVVVNDDVL TKIDRLADYA PLHNPANAMG IRAFQKLLPD ALSVAVFDTS FHQTMPEKNY 

       190        200        210        220        230        240 
LYSIPYEYYA RYGARKYGAH GTSHRYVTER AAKKLDIPLD EFNAISFHLG AGASITAIKN 

       250        260        270        280        290        300 
GKSYDTSMGF TPLAGLTMAT RSGDVDPSLV YYIQEREGLS NEEMLSVLNK KSGLLGISTI 

       310        320        330        340        350        360 
SSDMRDLEEV QETNTHAKLA LDMFYDRVIR YAGQYFAELG RVDAVIFTAG IGENDAVTRA 

       370        380        390        400        410 
KVLESLAFAG VKLDAEANNV RGKEAILTTD DSSVTGLLIP TNEELMIARD VEALR

« Hide

References

[1]"Complete genome sequence analysis of Leuconostoc kimchii IMSNU 11154."
Oh H.M., Cho Y.J., Kim B.K., Roe J.H., Kang S.O., Nahm B.H., Jeong G., Han H.U., Chun J.
J. Bacteriol. 192:3844-3845(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IMSNU 11154 / KCTC 2386 / IH25.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001758 Genomic DNA. Translation: ADG41525.1.
RefSeqYP_003622494.1. NC_014136.1.

3D structure databases

ProteinModelPortalD5T4Q4.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADG41525; ADG41525; LKI_09930.
GeneID9134573.
KEGGlki:LKI_09930.
PATRIC38188563. VBILeuKim161478_1933.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000288398.
KOK00925.

Enzyme and pathway databases

BioCycLKIM762051:GJOL-2061-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 nameD5T4Q4_LEUKI
AccessionPrimary (citable) accession number: D5T4Q4
Entry history
Integrated into UniProtKB/TrEMBL: July 13, 2010
Last sequence update: July 13, 2010
Last modified: July 9, 2014
This is version 30 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