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G0CIJ9 (G0CIJ9_XANCA) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 18. 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:acsA HAMAP-Rule MF_01123 EMBL AEL05124.1
ORF Names:XCR_0194 EMBL AEL05124.1
OrganismXanthomonas campestris pv. raphani 756C [Complete proteome] EMBL AEL05124.1
Taxonomic identifier990315 [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 SAAS SAAS011904

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

Region410 – 4156Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5161 By similarity HAMAP-Rule MF_01123
Metal binding5361Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5381Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5411Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3101Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3341Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3861Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site4991Substrate By similarity HAMAP-Rule MF_01123
Binding site5141Substrate By similarity HAMAP-Rule MF_01123
Binding site5221Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5251Substrate By similarity HAMAP-Rule MF_01123
Binding site5831Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6081N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
G0CIJ9 [UniParc].

Last modified October 19, 2011. Version 1.
Checksum: 6082B9B0D07F9F54

FASTA64771,352
        10         20         30         40         50         60 
MADVYPVDPA FAAGARITRE 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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002789 Genomic DNA. Translation: AEL05124.1.
RefSeqYP_005635242.1. NC_017271.1.

3D structure databases

ProteinModelPortalG0CIJ9.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEL05124; AEL05124; XCR_0194.
GeneID12263339.
KEGGxcp:XCR_0194.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01895.

Enzyme and pathway databases

BioCycXCAM990315:GLMR-194-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 nameG0CIJ9_XANCA
AccessionPrimary (citable) accession number: G0CIJ9
Entry history
Integrated into UniProtKB/TrEMBL: October 19, 2011
Last sequence update: October 19, 2011
Last modified: July 9, 2014
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)