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Q4UP35 (ACSA_XANC8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:XC_4149
OrganismXanthomonas campestris pv. campestris (strain 8004) [Complete proteome] [HAMAP]
Taxonomic identifier314565 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length647 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 – 647647Acetyl-coenzyme A synthetase HAMAP MF_01123
PRO_1000085007

Sites

Active site5161 By similarity

Amino acid modifications

Modified residue6081N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4UP35 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: B29E360F8DDC9F54

FASTA64771,410
        10         20         30         40         50         60 
MADVYPVDPA FAADARITRE QYATLYRESI EHPEQFWGKA AQRLDWFKQP TQIKDVSFAL 

        70         80         90        100        110        120 
DDFHVRWFGD GELNASVNCL DRQLATRGDK TALLFEPDSP DSPSYPVTYR ELYERVCKLG 

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

       190        200        210        220        230        240 
LIITADEGLR GGKKIPLKAN VDAALKIPGT NTVETVLVVR HTGGAVDMQA 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 
RALMREGEAP VKKTSRSSLR LLGSVGEPIN PEAWRWYYEV VGDSRCPIVD TWWQTETGGI 

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

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

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

       610        620        630        640 
LPKTRSGKIM RRILRKIAEN APDQLGDTST LADPSVVDSL VNERLTR 

« Hide

References

[1]"Comparative and functional genomic analyses of the pathogenicity of phytopathogen Xanthomonas campestris pv. campestris."
Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q., Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S., Gu W.-Y., Lu G., Rong L. expand/collapse author list , Tian Y., Yao Z., Fu G., Chen B., Fang R., Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.
Genome Res. 15:757-767(2005) [PubMed: 15899963] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 8004.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000050 Genomic DNA. Translation: AAY51188.1.
RefSeqYP_245208.1. NC_007086.1.

3D structure databases

ProteinModelPortalQ4UP35.
SMRQ4UP35. Positions 9-644.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ4UP35.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3379768.
GenomeReviewsGene locus XC_4149 in contig CP000050_GR.
KEGGxcb:XC_4149.
PATRIC24070097. VBIXanCam24967_4400.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHBG547964.
OMAHQRMVDT.
PhylomeDBQ4UP35.
ProtClustDBPRK00174.

Enzyme and pathway databases

BioCycXCAM314565:XC_4149-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_XANC8
AccessionPrimary (citable) accession number: Q4UP35
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 5, 2005
Last modified: January 25, 2012
This is version 40 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