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Q2NXE2 (ACSA_XANOM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. 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:XOO4280
OrganismXanthomonas oryzae pv. oryzae (strain MAFF 311018) [Complete proteome] [HAMAP]
Taxonomic identifier342109 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length647 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 – 647647Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123
PRO_1000085008

Regions

Region410 – 4156Substrate binding By similarity

Sites

Active site5161 By similarity
Metal binding5361Magnesium; via carbonyl oxygen By similarity
Metal binding5381Magnesium; via carbonyl oxygen By similarity
Metal binding5411Magnesium; via carbonyl oxygen By similarity
Binding site3101Coenzyme A By similarity
Binding site3341Coenzyme A By similarity
Binding site3861Substrate; via amide nitrogen By similarity
Binding site4991Substrate By similarity
Binding site5141Substrate By similarity
Binding site5221Coenzyme A By similarity
Binding site5251Substrate By similarity
Binding site5831Coenzyme A

Amino acid modifications

Modified residue6081N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2NXE2 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 33558E37802A2523

FASTA64771,366
        10         20         30         40         50         60 
MADVYPVDPA FAADARVTRE QYAALYRESI EHPEQFWGKA AQRLEWFKQP TQVKDVSYAL 

        70         80         90        100        110        120 
DDFHIRWFGD GELNASVNCL DRQLATRGDK TALLFEPDSP DAASYPVTYR QLYERVCKLG 

       130        140        150        160        170        180 
NALRNLGVKK GDRVTIYLPM IVDAAVAMLA CARIGAVHSV VFGGFAANSI ADRVIDCQSK 

       190        200        210        220        230        240 
LIITADEGLR GGKKIPLKAN VDAALKIPGT NTIETVLVVR HTGGAVEMQA PRDRWFHDVV 

       250        260        270        280        290        300 
DGQPAECEPE RMNAEDPLFI LYTSGSTGKP KGVLHTTAGY LLFASYTHEV VFDLREDDIY 

       310        320        330        340        350        360 
WCTADVGWVT GHSYIVYGPL ANGATAVMFE GVPNYPNVSR FWEVIDKHQV TIFYTAPTAI 

       370        380        390        400        410        420 
RALMRDGAEP VKKTSRKSLR LLGSVGEPIN PEAWRWYYDV VGDSRCPIVD TWWQTETGGI 

       430        440        450        460        470        480 
LISPLAGAVD LKPGSATLPF FGVQPALVDA EGKILEGATE GNLVLLDSWP GQMRSVYGDH 

       490        500        510        520        530        540 
QRFIDTYFRT YPGSYFTGDG CRRDADGYYW ITGRVDDVIN VSGHRIGTAE VESALVSHPK 

       550        560        570        580        590        600 
VAEAAVVGFP HDVKGQGIYA YVTLIAGETP SDELHKELVS WVRKEIGPIA SPDHLQWAPG 

       610        620        630        640 
LPKTRSGKIM RRILRKIAEN APDQLGDTST LADPSVVDSL VNERLTR 

« Hide

References

[1]"Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of large numbers of effector genes and insertion sequences to its race diversity."
Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.
Jpn. Agric. Res. Q. 39:275-287(2005)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF 311018.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008229 Genomic DNA. Translation: BAE71035.1.
RefSeqYP_453309.1. NC_007705.1.

3D structure databases

ProteinModelPortalQ2NXE2.
SMRQ2NXE2. Positions 9-644.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING342109.XOO_4280.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE71035; BAE71035; BAE71035.
GeneID3859446.
KEGGxom:XOO_4280.
PATRIC24119017. VBIXanOry49434_4911.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000128470.
KOK01895.
OMARRIFEPT.
OrthoDBEOG68WR2H.

Enzyme and pathway databases

BioCycXORY342109:GIX9-4339-MONOMER.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
InterProIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
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.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACSA_XANOM
AccessionPrimary (citable) accession number: Q2NXE2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 7, 2006
Last modified: May 14, 2014
This is version 57 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