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B2SU07 (B2SU07_XANOP) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 46. 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 ACD61559.1
Ordered Locus Names:PXO_03257 EMBL ACD61559.1
OrganismXanthomonas oryzae pv. oryzae (strain PXO99A) [Complete proteome] [HAMAP] EMBL ACD61559.1
Taxonomic identifier360094 [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
B2SU07 [UniParc].

Last modified July 1, 2008. 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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000967 Genomic DNA. Translation: ACD61559.1.
RefSeqYP_001916091.1. NC_010717.1.

3D structure databases

ProteinModelPortalB2SU07.
SMRB2SU07. Positions 9-644.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360094.PXO_03257.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD61559; ACD61559; PXO_03257.
GeneID6308552.
KEGGxop:PXO_03257.
PATRIC24129651. VBIXanOry73153_5152.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMATGSEVPW.
OrthoDBEOG68WR2H.

Enzyme and pathway databases

BioCycXORY360094:GI45-5032-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 nameB2SU07_XANOP
AccessionPrimary (citable) accession number: B2SU07
Entry history
Integrated into UniProtKB/TrEMBL: July 1, 2008
Last sequence update: July 1, 2008
Last modified: June 11, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)