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C1DFK2 (C1DFK2_AZOVD) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 38. 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
Synonyms:acsA2 EMBL ACO80398.1
Ordered Locus Names:Avin_42750 EMBL ACO80398.1
OrganismAzotobacter vinelandii (strain DJ / ATCC BAA-1303) [Complete proteome] [HAMAP] EMBL ACO80398.1
Taxonomic identifier322710 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Protein attributes

Sequence length645 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

Region408 – 4136Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5141 By similarity HAMAP-Rule MF_01123
Metal binding5341Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5361Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5391Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3081Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3321Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3841Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site4971Substrate By similarity HAMAP-Rule MF_01123
Binding site5121Substrate By similarity HAMAP-Rule MF_01123
Binding site5201Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5231Substrate By similarity HAMAP-Rule MF_01123
Binding site5811Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6061N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
C1DFK2 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 2196F80A1AE5C342

FASTA64571,897
        10         20         30         40         50         60 
MFKIANHPVS EALRQHSWLN NDDYLRLYRQ SVEQPDSFWA EQATLFLDWF KPWRNIHRGD 

        70         80         90        100        110        120 
MNKGEIHWFE GSQLNVAHNC IDRHLKQRGD QVAIIWEGDN PADSARITYR QLHEQVCRLA 

       130        140        150        160        170        180 
NLLKSRGIGK GDRVCIYMPM IPEAAYAMLA CARIGAVHSV VFGGFSPEAL RDRILDADCR 

       190        200        210        220        230        240 
LLITADESVR GGKVVPLKRN ADKALQSCSG VSSVIVVRRT GGAIDWNVGR DLWYHEAVPG 

       250        260        270        280        290        300 
CSADCPAEPM DAEAPLFILY TSGSTGKPKG VLHTTGGYLL QAAMTHQYVF DYHDGDIYWC 

       310        320        330        340        350        360 
SADIGWITGH SYIVYGPLAN GATTLIFEGV PNYPDASRFW QVVDKHRVNI FYTAPTALRS 

       370        380        390        400        410        420 
LMREGEGPVR KTSRASLRLL GSVGEPINPE AWEWYYHVVG DSRCPIVDTW WQTETGAIMI 

       430        440        450        460        470        480 
TPLPGATLLK PGSATRPFFG VQPVLLDDKG KEIEGPGAGI LAIKASWPSQ IRSIYGDHQR 

       490        500        510        520        530        540 
LIDTYFKPCP GYYFTGDGAR RDEDGYYWIT GRVDDVINVS GHRIGTAEVE SALVLHDSIA 

       550        560        570        580        590        600 
EAAVVGCPHD VKGQCVYAFV TLVTGSRPSD QLKRELIDQV SREIGGFAKP DFLQWAPRLP 

       610        620        630        640 
KTRSGKIMRR ILRKIACNEL DNLGDTSTLS DPSVLQELID NRLSH 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001157 Genomic DNA. Translation: ACO80398.1.
RefSeqYP_002801373.1. NC_012560.1.

3D structure databases

ProteinModelPortalC1DFK2.
SMRC1DFK2. Positions 7-642.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING322710.Avin_42750.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO80398; ACO80398; Avin_42750.
GeneID7763150.
KEGGavn:Avin_42750.
PATRIC21034580. VBIAzoVin72790_4023.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAKSLENPE.
OrthoDBEOG68WR2H.

Enzyme and pathway databases

BioCycAVIN322710:GJ0M-4277-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 nameC1DFK2_AZOVD
AccessionPrimary (citable) accession number: C1DFK2
Entry history
Integrated into UniProtKB/TrEMBL: May 26, 2009
Last sequence update: May 26, 2009
Last modified: June 11, 2014
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)