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Q5GU25 (Q5GU25_XANOR) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 53. 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-Rule MF_01123

Short name=AcCoA synthetase HAMAP-Rule MF_01123
Short name=Acs HAMAP-Rule MF_01123
EC=6.2.1.1 HAMAP-Rule MF_01123
Alternative name(s):
Acetate--CoA ligase HAMAP-Rule MF_01123
Acyl-activating enzyme HAMAP-Rule MF_01123
Gene names
Name:acs EMBL AAW77798.1
Synonyms:acsA HAMAP-Rule MF_01123
Ordered Locus Names:XOO4544 EMBL AAW77798.1
OrganismXanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85) [Complete proteome] [HAMAP] EMBL AAW77798.1
Taxonomic identifier291331 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length696 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. HAMAP-Rule MF_01123

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region459 – 4646Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5651 By similarity HAMAP-Rule MF_01123
Metal binding5851Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5871Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5901Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3591Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3831Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site4351Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5481Substrate By similarity HAMAP-Rule MF_01123
Binding site5631Substrate By similarity HAMAP-Rule MF_01123
Binding site5711Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5741Substrate By similarity HAMAP-Rule MF_01123
Binding site6321Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6571N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
Q5GU25 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 79025F1A1D84B06A

FASTA69676,479
        10         20         30         40         50         60 
MCAGALPGGL RPRSKAPLAV GTEWMRHTDC LPREAVTPSS DKFIASEGAM ADVYPVDPAF 

        70         80         90        100        110        120 
AADARVTREQ YAALYRESIE HPEQFWGKAA QRLEWFKQPT QVKDVSYALD DFHIRWFGDG 

       130        140        150        160        170        180 
ELNASVNCLD RQLATRGDKT ALLFEPDSPD AASYPVTYRQ LYERVCKLGN ALRNLGVKKG 

       190        200        210        220        230        240 
DRVTIYLPMI VDAAVAMLAC ARIGAVHSVV FGGFAANSIA DRVIDCQSKL IITADEGLRG 

       250        260        270        280        290        300 
GKKIPLKANV DAALKIPGTN TIETVLVVRH TGGAVEMQAP RDRWFQDVVD GQPAECEPER 

       310        320        330        340        350        360 
MNAEDPLFIL YTSGSTGKPK GVLHTTAGYL LFASYTHEVV FDLREDDIYW CTADVGWVTG 

       370        380        390        400        410        420 
HSYIVYGPLA NGATAVMFEG VPNYPNVSRF WEVIDKHQVT IFYTAPTAIR ALMRDGAEPV 

       430        440        450        460        470        480 
KKTSRKSLRL LGSVGEPINP EAWRWYYDVV GDSRCPIVDT WWQTETGGIL ISPLAGAVDL 

       490        500        510        520        530        540 
KPGSATLPFF GVQPALVDAE GKILEGATEG NLVLLDSWPG QMRSVYGDHQ RFIDTYFRTY 

       550        560        570        580        590        600 
PGSYFTGDGC RRDADGYYWI TGRVDDVINV SGHRIGTAEV ESALVSHPKV AEAAVVGFPH 

       610        620        630        640        650        660 
DVKGQGIYAY VTLIAGETPS DELHKELVSW VRKEIGPIAS PDHLQWAPGL PKTRSGKIMR 

       670        680        690 
RILRKIAENA PDQLGDTSTL ADPSVVDSLV NERLTR 

« Hide

References

[1]"The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the bacterial blight pathogen of rice."
Lee B.M., Park Y.J., Park D.S., Kang H.W., Kim J.G., Song E.S., Park I.C., Yoon U.H., Hahn J.H., Koo B.S., Lee G.B., Kim H., Park H.S., Yoon K.O., Kim J.H., Jung C.H., Koh N.H., Seo J.S., Go S.J.
Nucleic Acids Res. 33:577-586(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KACC10331 / KXO85.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013598 Genomic DNA. Translation: AAW77798.1.
RefSeqYP_203183.1. NC_006834.1.

3D structure databases

ProteinModelPortalQ5GU25.
SMRQ5GU25. Positions 58-693.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING291331.XOO4544.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW77798; AAW77798; XOO4544.
GeneID3262868.
KEGGxoo:XOO4544.
PATRIC24108869. VBIXanOry111333_5045.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000229981.
KOK01895.
OMAYGDHQRM.
OrthoDBEOG68WR2H.
ProtClustDBPRK00174.

Enzyme and pathway databases

BioCycXORY291331:GJBV-4197-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 nameQ5GU25_XANOR
AccessionPrimary (citable) accession number: Q5GU25
Entry history
Integrated into UniProtKB/TrEMBL: March 1, 2005
Last sequence update: March 1, 2005
Last modified: April 16, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)