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C8X4E2 (C8X4E2_DESRD) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 31. 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:Dret_2132 EMBL ACV69416.1
OrganismDesulfohalobium retbaense (strain DSM 5692) [Complete proteome] [HAMAP] EMBL ACV69416.1
Taxonomic identifier485915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfohalobiaceaeDesulfohalobium

Protein attributes

Sequence length661 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

Region203 – 2064Coenzyme A By similarity HAMAP-Rule MF_01123
Region422 – 4276Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5281 By similarity HAMAP-Rule MF_01123
Metal binding5481Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5501Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5531Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3221Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3981Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5111Substrate By similarity HAMAP-Rule MF_01123
Binding site5261Substrate By similarity HAMAP-Rule MF_01123
Binding site5341Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5371Substrate By similarity HAMAP-Rule MF_01123
Binding site5951Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6201N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
C8X4E2 [UniParc].

Last modified November 3, 2009. Version 1.
Checksum: 0B1F90A93F31B941

FASTA66173,245
        10         20         30         40         50         60 
MGGSDEHIES MMHERRHFPP PRHGSERAHI PGPEAYDDLR DQAARDPEGF WAERAKALLD 

        70         80         90        100        110        120 
WDSEWDTVLE ADWETPEFKW FAGGKLNACA NCLDRHVASG RGEKTALIWQ GEPEDDVRQF 

       130        140        150        160        170        180 
TYAELRDEVV KFAKVLKKWG VGKGDRVAVY LPMIPELPIA MLACARIGAV HSVVFAGFSA 

       190        200        210        220        230        240 
HSLQNRIQDC EAKVLITADA VIRAGKQIPL KTNGDEALEA CPSVEHCIVV NRAGLDVAMH 

       250        260        270        280        290        300 
EGRDVWWHDA VAGDDGTDCP PESMDAEDLL FILYTSGSTG KPKGVVHTTG GYLTYTAQTT 

       310        320        330        340        350        360 
QWVFDIQEDD VYWCTADIGW ITGHSYILYG PLALGATTVM FEGVPSYPQP DRFWQVVEKF 

       370        380        390        400        410        420 
KVTIFYTAPT VIRALMREGP QWTETRDLSS LRLLGSVGEP INPEAWMWYH DHVGKGELPV 

       430        440        450        460        470        480 
LDTWWQTETG GIMISAVPYA TTLKPGSASQ PLPGIEADIV DRDGEPVGPN RGGHLVVKTP 

       490        500        510        520        530        540 
WPGMLRNVYG DPARYKSTYF ERFPGMYESG DSARMDEEGY FWIMGRLDDV INVSGHRLGT 

       550        560        570        580        590        600 
AEIESALVAH EAVAEAAVVG MPHEVKGQAI YAYVTLKSTF QENDELRKVL RQHVRTEIGA 

       610        620        630        640        650        660 
IATPEIIQFA PGLPKTRSGK IMRRILRKIA ADETNAFGDT STLADPTVIA DLIDGKNLLG 


K 

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References

[1]"The complete chromosome of Desulfohalobium retbaense DSM 5692."
US DOE Joint Genome Institute (JGI-PGF)
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R. expand/collapse author list , Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Klenk H.-P., Eisen J.A.
Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 5692.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001734 Genomic DNA. Translation: ACV69416.1.
RefSeqYP_003198994.1. NC_013223.1.

3D structure databases

ProteinModelPortalC8X4E2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING485915.Dret_2132.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACV69416; ACV69416; Dret_2132.
GeneID8419982.
KEGGdrt:Dret_2132.
PATRIC21701382. VBIDesRet71890_2248.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAKIATHND.
OrthoDBEOG68WR2H.
ProtClustDBCLSK706078.

Enzyme and pathway databases

BioCycDRET485915:GHRJ-2180-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 nameC8X4E2_DESRD
AccessionPrimary (citable) accession number: C8X4E2
Entry history
Integrated into UniProtKB/TrEMBL: November 3, 2009
Last sequence update: November 3, 2009
Last modified: February 19, 2014
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)