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A9IIL7 (A9IIL7_BORPD) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 44. 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
Ordered Locus Names:Bpet1782 EMBL CAP42121.1
OrganismBordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]
Taxonomic identifier340100 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length659 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 SAAS020845

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

Region422 – 4276Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5291 By similarity HAMAP-Rule MF_01123
Metal binding5491Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5511Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5541Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3181Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3981Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5121Substrate By similarity HAMAP-Rule MF_01123
Binding site5271Substrate By similarity HAMAP-Rule MF_01123
Binding site5351Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5381Substrate By similarity HAMAP-Rule MF_01123
Binding site5991Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6241N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
A9IIL7 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: B9F6B19C56639FE2

FASTA65972,328
        10         20         30         40         50         60 
MSNTIESVLV ETRVFPPPER AAQGARIGSM DAYRALCQEV EQDFDGFWTR QARENLTWSK 

        70         80         90        100        110        120 
PFTQVLDESN APFYRWFGDG ELNVSANCLD VHLNNGNADK TAIIFESDDG KVDKVTYREL 

       130        140        150        160        170        180 
LARVCRFANG LKSLGYKKGD RAIIYMPMSI QAVVAMQACA RLGVTHSVVF GGFSAKSLQE 

       190        200        210        220        230        240 
RIVDVGASLV ITADEQVRGG KTIPLKPAVE EAIGMGGCDA VTKIVVYKRT GGNVPWQDGR 

       250        260        270        280        290        300 
DLWMHDVEAG QPDTCEPVPV NAEHPLFILY TSGSTGKPKG VQHSSGGYLL WALLTVKWTF 

       310        320        330        340        350        360 
DARPDDVYWC TADVGWVTGH TYITYGPLAA GLTQIVFEGV PTYPDAGRFW DMIARHKVTT 

       370        380        390        400        410        420 
FYTAPTAIRS LIKASEATPA AHPRNYDLNS LRIIGTVGEP INPEAWVWYH KNVGQERCPI 

       430        440        450        460        470        480 
VDTWWQTETG GHMINPLPGA TPTKPGSCTL PLPGIAATVV DETGAEVEPG NGGFLAIKRP 

       490        500        510        520        530        540 
WPAMIRTIWG DPERFKKSYF PPELRGYYLA GDGAQRDADG YFWIMGRIDD VLNVSGHRLG 

       550        560        570        580        590        600 
TMEVESALVS HELVAEAAVV GRPDDTTGEA VVAFVVLKRA RPEGDEAQAI AKQLRDWVGK 

       610        620        630        640        650 
EIGPIAKPKD IRFGDNLPKT RSGKIMRRLL RVVAKGEQIT QDVSTLENPA ILDQLAKSV 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM902716 Genomic DNA. Translation: CAP42121.1.
RefSeqYP_001630390.1. NC_010170.1.

3D structure databases

ProteinModelPortalA9IIL7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING340100.Bpet1782.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAP42121; CAP42121; Bpet1782.
GeneID5821098.
KEGGbpt:Bpet1782.
PATRIC21165015. VBIBorPet31633_1772.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAYGDHQRM.
OrthoDBEOG68WR2H.
ProtClustDBPRK00174.

Enzyme and pathway databases

BioCycBPET340100:GJBO-1806-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 nameA9IIL7_BORPD
AccessionPrimary (citable) accession number: A9IIL7
Entry history
Integrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: February 19, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)