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B0T280 (B0T280_CAUSK) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 42. 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:Caul_0111 EMBL ABZ69249.1
OrganismCaulobacter sp. (strain K31) [Complete proteome] [HAMAP] EMBL ABZ69249.1
Taxonomic identifier366602 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter

Protein attributes

Sequence length646 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

Region409 – 4146Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5151 By similarity HAMAP-Rule MF_01123
Metal binding5351Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5371Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5401Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3091Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3331Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3851Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site4981Substrate By similarity HAMAP-Rule MF_01123
Binding site5131Substrate By similarity HAMAP-Rule MF_01123
Binding site5211Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5241Substrate By similarity HAMAP-Rule MF_01123
Binding site5821Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6071N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
B0T280 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 1AA950EAE622162D

FASTA64670,982
        10         20         30         40         50         60 
MSDGQVFPIP DDWAGKAHID AAGYEAALAR VEADPEGYWR DLAGRLDWIR APTQIKDVSF 

        70         80         90        100        110        120 
AKDDFRIHWY ADGVLNVSAN CIDRHLPHRK DEVALIFEGD EPGVSSTLTY GQLHEEVCRM 

       130        140        150        160        170        180 
ANVLKVQGVR KGDRVTIYLP MIPIAAVAML ACARIGAVHS VVFGGFSPDS IAGRIQDCGS 

       190        200        210        220        230        240 
HFVITADEGR RGGKRVPLKA NIDKALEHCP WVSKVLMVRW TGAETTLVRH RDVVWEDVKD 

       250        260        270        280        290        300 
SVSADCPPEP MNAEDPLFIL YTSGSTGKPK GVLHTTGGYL AWAAWTHEAV FDYRPGEVFW 

       310        320        330        340        350        360 
CTADVGWVTG HSYVVYGPLA NGGTSLIFEG VPNYPTPARF WEVVDKHQVE IFYTAPTALR 

       370        380        390        400        410        420 
ALMREGDDWV TKNDLSSLRL LGSVGEPINP EAWLWYHRVV GKDRLPIVDT WWQTETGGVL 

       430        440        450        460        470        480 
VSPLPGATAL KPGSATKPLP GVKLQLVDAE GHVLEGATEG NLLITDSWPG QMRTVYGDHG 

       490        500        510        520        530        540 
RFFDTYFSAY PGKYFTGDGC RRDADGYYWI TGRVDDVINV SGHRLGTAEI ESALVAHDTV 

       550        560        570        580        590        600 
AEAAVVGYPH DIKGQGVYAY VTLRAGVEPT DSLRKDLMLW VRQEIGPFAA PDVLQWAPGL 

       610        620        630        640 
PKTRSGKIMR RILRKIAENE LGSLGDISTL ADPSVVDDLV KNRANS 

« Hide

References

[1]"Complete sequence of chromosome of Caulobacter sp. K31."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Kim E., Stephens C., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K31 EMBL ABZ69249.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000927 Genomic DNA. Translation: ABZ69249.1.
RefSeqYP_001681747.1. NC_010338.1.

3D structure databases

ProteinModelPortalB0T280.
SMRB0T280. Positions 9-643.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING366602.Caul_0111.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABZ69249; ABZ69249; Caul_0111.
GeneID5897823.
KEGGcak:Caul_0111.
PATRIC21313238. VBICauSp18104_0493.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAYWDIIER.
OrthoDBEOG68WR2H.
ProtClustDBPRK00174.

Enzyme and pathway databases

BioCycCSP366602:GH0Y-112-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 nameB0T280_CAUSK
AccessionPrimary (citable) accession number: B0T280
Entry history
Integrated into UniProtKB/TrEMBL: April 8, 2008
Last sequence update: April 8, 2008
Last modified: February 19, 2014
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)