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Q4FVA1 (ACSA_PSYA2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Acetyl-coenzyme A synthetase

EC=6.2.1.1
Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme
Gene names
Name:acsA
Ordered Locus Names:Psyc_0184
OrganismPsychrobacter arcticus (strain DSM 17307 / 273-4) [Complete proteome] [HAMAP]
Taxonomic identifier259536 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter

Protein attributes

Sequence length653 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP MF_01123

Post-translational modification

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity. HAMAP MF_01123

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular functionAMP binding

Inferred from electronic annotation. Source: InterPro

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

acetate-CoA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 653653Acetyl-coenzyme A synthetase HAMAP MF_01123
PRO_1000137272

Sites

Active site5191 By similarity

Amino acid modifications

Modified residue6111N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4FVA1 [UniParc].

Last modified August 30, 2005. Version 1.
Checksum: 66ADF5B698220AE0

FASTA65372,059
        10         20         30         40         50         60 
MTQKSFPITP EFLAAANVTA EQYVEQYQQS IASPEATDAF WAKQAELIDW IKKPTKISDV 

        70         80         90        100        110        120 
SYDLEDFRIK WFEDGELNIS VNCLDRHVKN NPYKPAIIWE GDHPSLHKII SFKELHEAVC 

       130        140        150        160        170        180 
RLGNAMRKLG VKKGDRVTLY MPMIPEAVVA MLACTRIGAV HSVVFGGFST QSLGNRIIDS 

       190        200        210        220        230        240 
QSKLVITADE GIRGNKRTPL KANVDRALDM DGTDSVSNVI VVHRTGNSVP MSGRRDIWYH 

       250        260        270        280        290        300 
SLVDGESQYC EPEVMNAEDP LFLLYTSGST GKPKGVLHTT GGYITYALST FRDVFDVKDD 

       310        320        330        340        350        360 
DVYWCTADVG WVTGHTYATY APLANGTTTV MFEGVPEYPT WARIGHIIDK HQITVLYTAP 

       370        380        390        400        410        420 
TAIRAMMKEG DTFVRESDRS SLRLLGTVGE PINPEAWDWY YHIVGGGKCP VVDTWWQTET 

       430        440        450        460        470        480 
GGIMLAPIPG TVAMKPGAVM NPLYGIIPEV IDTDGVALEG AAEGNLVING SWPGQMRTIY 

       490        500        510        520        530        540 
KDHARFLETY FTEYPGYYFT GDGVQRDEDG HYWITGRVDD VLNVSGHRLG TAEIESAIVA 

       550        560        570        580        590        600 
HPATAEAAVV GMPHDIRGIG ICAFVILKSS ETATESLKAE LNRHVRTEIG PIANLDAIYM 

       610        620        630        640        650 
VNVLPKTRSG KIMRRILRSL AAGQYVGLGD LSTLADSSVI NELVEVVKTE RAK 

« Hide

References

[1]"The genome sequence of Psychrobacter arcticus 273-4, a psychroactive Siberian permafrost bacterium, reveals mechanisms for adaptation to low-temperature growth."
Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P., Murray A., Thomashow M., Tiedje J.M.
Appl. Environ. Microbiol. 76:2304-2312(2010) [PubMed: 20154119] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17307 / 273-4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000082 Genomic DNA. Translation: AAZ18057.1.
RefSeqYP_263491.1. NC_007204.1.

3D structure databases

ProteinModelPortalQ4FVA1.
SMRQ4FVA1. Positions 7-648.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ4FVA1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3514221.
GenomeReviewsGene locus Psyc_0184 in contig CP000082_GR.
KEGGpar:Psyc_0184.
NMPDRfig|259536.4.peg.347.
PATRIC23054561. VBIPsyArc98534_0221.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHBG547964.
OMAKGKPYML.
PhylomeDBQ4FVA1.
ProtClustDBPRK00174.

Enzyme and pathway databases

BioCycPARC259536:PSYC_0184-MONOMER.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
[Tree]
InterProIPR011904. Ac_CoA_lig.
IPR024597. Acyl-CoA_synth_DUF3448.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
KOK01895.
PANTHERPTHR24095:SF42. PTHR24095:SF42. 1 hit.
PfamPF00501. AMP-binding. 1 hit.
PF11930. DUF3448. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACSA_PSYA2
AccessionPrimary (citable) accession number: Q4FVA1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: August 30, 2005
Last modified: January 25, 2012
This is version 44 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