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B0RYU5 (B0RYU5_XANCB) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acetyl-coenzyme A synthetase HAMAP MF_01123

EC=6.2.1.1 HAMAP MF_01123
Alternative name(s):
Acetate--CoA ligase HAMAP MF_01123
Acyl-activating enzyme HAMAP MF_01123
Gene names
Name:acsA HAMAP MF_01123 EMBL CAP53631.1
Ordered Locus Names:xcc-b100_4261
OrganismXanthomonas campestris pv. campestris (strain B100) [Complete proteome] [HAMAP]
Taxonomic identifier509169 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length672 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. HAMAP MF_01123

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site5411 By similarity HAMAP MF_01123

Amino acid modifications

Modified residue6331N6-acetyllysine By similarity HAMAP MF_01123

Sequences

Sequence LengthMass (Da)Tools
B0RYU5 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: C1DB0AB7331FB307

FASTA67274,148
        10         20         30         40         50         60 
MRHTDCLRGA RKRPSSDKLI ASEGAMADVY PVDPAFAADA RITREQYATL YRESIEHPEQ 

        70         80         90        100        110        120 
FWGKAAQRLD WFKQPTQIKD VSFALDDFHV RWFGDGELNA SVNCLDRQLA TRGDKTALLF 

       130        140        150        160        170        180 
EPDSPDSPSY PVTYRELYER VCKLGNALRN LGVKKGDRVT IYLPMIVDAA VAMLACARIG 

       190        200        210        220        230        240 
AVHSVVFGGF AANSIADRVI DCQSKLIITA DEGLRGGKKI PLKANVDAAL KIPGTNTVET 

       250        260        270        280        290        300 
VLVVRHTGGA VDMQAPRDRW FHDVVDGQPA ECEPERMNAE DPLFILYTSG STGKPKGVLH 

       310        320        330        340        350        360 
TTAGYLLFAS YTHEVVFDLR EDDIYWCTAD VGWVTGHSYI VYGPLANGAT AVMFEGVPNY 

       370        380        390        400        410        420 
PNVSRFWEVI DKHQVTIFYT APTAIRALMR EGEAPVKKTS RSSLRLLGSV GEPINPEAWR 

       430        440        450        460        470        480 
WYYEVVGDSR CPIVDTWWQT ETGGILISPL AGAVDLKPGS ATLPFFGVQP ALVDAEGKIL 

       490        500        510        520        530        540 
EGATEGNLVL LDSWPGQMRT VYGDHQRFID TYFRTYPGSY FTGDGCRRDA DGYYWITGRV 

       550        560        570        580        590        600 
DDVINVSGHR IGTAEVESAL VSHPKVAEAA VVGFPHDVKG QGIYAYVTLI AGETPSEELH 

       610        620        630        640        650        660 
KELVSWVRKE IGPIASPDHL QWAPGLPKTR SGKIMRRILR KIAENAPDQL GDTSTLADPS 

       670 
VVDSLVNERL TR 

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References

[1]"The genome of Xanthomonas campestris pv. campestris B100 and its use for the reconstruction of metabolic pathways involved in xanthan biosynthesis."
Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T., Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K., Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K., Puehler A.
J. Biotechnol. 134:33-45(2008) [PubMed: 18304669] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM920689 Genomic DNA. Translation: CAP53631.1.
RefSeqYP_001905666.1. NC_010688.1.

3D structure databases

ProteinModelPortalB0RYU5.
SMRB0RYU5. Positions 34-669.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0RYU5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6324038.
GenomeReviewsGene locus xcc-b100_4261 in contig AM920689_GR.
PATRIC24088543. VBIXanCam108527_4322.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG547964.
OMAHQRMVDT.
ProtClustDBPRK00174.

Enzyme and pathway databases

BioCycXCAM487884:XCC-B100_4261-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]
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 nameB0RYU5_XANCB
AccessionPrimary (citable) accession number: B0RYU5
Entry history
Integrated into UniProtKB/TrEMBL: April 8, 2008
Last sequence update: April 8, 2008
Last modified: December 14, 2011
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)