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A0QQK1 (ACKA_MYCS2) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetate kinase

EC=2.7.2.1
Alternative name(s):
Acetokinase
Gene names
Name:ackA
Ordered Locus Names:MSMEG_0784, MSMEI_0768
OrganismMycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Reference proteome] [HAMAP]
Taxonomic identifier246196 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length376 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 Probable. Ref.4

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00020.

Sequence similarities

Belongs to the acetokinase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacetyl-CoA biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

organic acid metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

acetate kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 376376Acetate kinase HAMAP-Rule MF_00020
PRO_0000421948

Regions

Nucleotide binding188 – 1925ATP HAMAP-Rule MF_00020
Nucleotide binding262 – 2643ATP HAMAP-Rule MF_00020
Nucleotide binding310 – 3145ATP HAMAP-Rule MF_00020

Sites

Active site1281Proton donor/acceptor By similarity
Metal binding71Magnesium By similarity
Metal binding3641Magnesium By similarity
Binding site141ATP By similarity
Binding site711Substrate By similarity
Site1601Transition state stabilizer By similarity
Site2211Transition state stabilizer By similarity

Secondary structure

................................................................. 376
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
A0QQK1 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 5F9BBCA380D2A161

FASTA37640,116
        10         20         30         40         50         60 
MTVLVVNSGS SSLKYAVVRP ASGEFLADGI IEEIGSGAVP DHDAALRAAF DELAAAGLHL 

        70         80         90        100        110        120 
EDLDLKAVGH RMVHGGKTFY KPSVVDDELI AKARELSPLA PLHNPPAIKG IEVARKLLPD 

       130        140        150        160        170        180 
LPHIAVFDTA FFHDLPAPAS TYAIDRELAE TWHIKRYGFH GTSHEYVSQQ AAIFLDRPLE 

       190        200        210        220        230        240 
SLNQIVLHLG NGASASAVAG GKAVDTSMGL TPMEGLVMGT RSGDIDPGVI MYLWRTAGMS 

       250        260        270        280        290        300 
VDDIESMLNR RSGVLGLGGA SDFRKLRELI ESGDEHAKLA YDVYIHRLRK YIGAYMAVLG 

       310        320        330        340        350        360 
RTDVISFTAG VGENVPPVRR DALAGLGGLG IEIDDALNSA KSDEPRLIST PDSRVTVLVV 

       370 
PTNEELAIAR ACVGVV 

« Hide

References

« Hide 'large scale' references
[1]Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[2]"Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[3]"Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[4]"Crystal structure of an acetate kinase from Mycobacterium smegmatis bound to AMP and sulfate."
Seattle structural genomics center for infectious disease (SSGCID)
Submitted (JAN-2013) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH AMP, SUBUNIT.
Strain: ATCC 700084 / mc(2)155.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000480 Genomic DNA. Translation: ABK74906.1.
CP001663 Genomic DNA. Translation: AFP37248.1.
RefSeqYP_006565543.1. NC_018289.1.
YP_885189.1. NC_008596.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4IJNX-ray1.70A/B2-376[»]
ProteinModelPortalA0QQK1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246196.MSMEG_0784.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK74906; ABK74906; MSMEG_0784.
AFP37248; AFP37248; MSMEI_0768.
GeneID4531693.
KEGGmsg:MSMEI_0768.
msm:MSMEG_0784.
PATRIC18074036. VBIMycSme59918_0779.

Phylogenomic databases

eggNOGCOG0282.
HOGENOMHOG000288399.
KOK00925.
OMAMIARETV.
OrthoDBEOG69975F.

Enzyme and pathway databases

BioCycMSME246196:GJ4Y-784-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 nameACKA_MYCS2
AccessionPrimary (citable) accession number: A0QQK1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2013
Last sequence update: January 9, 2007
Last modified: July 9, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways