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Q0AFF1 (ACSA_NITEC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. 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

Short name=AcCoA synthetase
Short name=Acs
EC=6.2.1.1
Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme
Gene names
Name:acsA
Ordered Locus Names:Neut_1690
OrganismNitrosomonas eutropha (strain C91) [Complete proteome] [HAMAP]
Taxonomic identifier335283 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas

Protein attributes

Sequence length655 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA By similarity. HAMAP-Rule MF_01123

Catalytic activity

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

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01123

Post-translational modification

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

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 655655Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123
PRO_1000065298

Regions

Region416 – 4216Substrate binding By similarity

Sites

Active site5251 By similarity
Metal binding5451Magnesium; via carbonyl oxygen By similarity
Metal binding5471Magnesium; via carbonyl oxygen By similarity
Metal binding5501Magnesium; via carbonyl oxygen By similarity
Binding site3161Coenzyme A By similarity
Binding site3921Substrate; via amide nitrogen By similarity
Binding site5081Substrate By similarity
Binding site5231Substrate By similarity
Binding site5311Coenzyme A By similarity
Binding site5341Substrate By similarity
Binding site5951Coenzyme A

Amino acid modifications

Modified residue6201N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0AFF1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: B81E66505C045F43

FASTA65573,338
        10         20         30         40         50         60 
MATIESILRE NRIFPPANEF VRHANITGMK TYEALRQEAE RDYAGFWAKL AKQYITWHKP 

        70         80         90        100        110        120 
FTRILDDTNP PFYKWFDDGE LNISWNCLDR HLTTQANKTA IIFESDEGEV IRCSYRELHQ 

       130        140        150        160        170        180 
RVCRFANGLK ALGIRQGDRI VIYMPMRIEA VVAMQACARI GVIHSVVFGG FSAKSVYERI 

       190        200        210        220        230        240 
IDAGASAVIT ADEQTRGGKR HALKATVDEA LAMGDTTSVH SVIVFRHTGT DIPWQPERDR 

       250        260        270        280        290        300 
WWHNLTASQS DECEPIWVNA EHPLFTLYTS GSTGKPKGVQ HSSAGYLLGA IVSMQWVFDY 

       310        320        330        340        350        360 
HSEDIFWCTA DVGWVTGHSY VTYGPLAIGA TQVIFEGTPT YPHAGRFWEI IQKHRVTTFY 

       370        380        390        400        410        420 
TAPTAIRSLI KLGPDLPEKY DLSSLRLLGS VGEPINPEAW MWYYTVIGQS RCPVVDTWWQ 

       430        440        450        460        470        480 
TETGSHMIAP IPGAIPAKPG SCTLPLPGID AAVVDETGLP AEQGKGGFLV IKRPFPSMLR 

       490        500        510        520        530        540 
TLWNDPERFR NTYFPADIAG GHYYLAGDSA HRDQDGYFWI MGRIDDVLNV SGHRLGTMEI 

       550        560        570        580        590        600 
ESALVAHPLV AEAAVVGKPH EIRGEVIVAF VVLRGKLPDD QQAAEIAETL REWVSSEIGA 

       610        620        630        640        650 
IARPEEIRFG ENLPKTRSGK LMRRLLRSLA RGETITQDIS TLENPVILEQ FSQTI 

« Hide

References

[1]"Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas eutropha C91: implications for niche adaptation."
Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S., Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.
Environ. Microbiol. 9:2993-3007(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C91.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000450 Genomic DNA. Translation: ABI59931.1.
RefSeqYP_747896.1. NC_008344.1.

3D structure databases

ProteinModelPortalQ0AFF1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335283.Neut_1690.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI59931; ABI59931; Neut_1690.
GeneID4273573.
KEGGnet:Neut_1690.
PATRIC22720832. VBINitEut7577_2068.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAYGDHQRM.
OrthoDBEOG68WR2H.
ProtClustDBPRK00174.

Enzyme and pathway databases

BioCycNEUT335283:GHT6-1724-MONOMER.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
InterProIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameACSA_NITEC
AccessionPrimary (citable) accession number: Q0AFF1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 17, 2006
Last modified: February 19, 2014
This is version 55 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