Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

E6S985 (E6S985_INTC7) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

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:Intca_0516 EMBL ADU47061.1
OrganismIntrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP) [Complete proteome] [HAMAP] EMBL ADU47061.1
Taxonomic identifier710696 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeIntrasporangiaceaeIntrasporangium

Protein attributes

Sequence length658 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

Region413 – 4186Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5191 By similarity HAMAP-Rule MF_01123
Metal binding5391Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5411Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5441Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3131Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3891Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5021Substrate By similarity HAMAP-Rule MF_01123
Binding site5171Substrate By similarity HAMAP-Rule MF_01123
Binding site5251Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5281Substrate By similarity HAMAP-Rule MF_01123
Binding site5931Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6181N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
E6S985 [UniParc].

Last modified March 8, 2011. Version 1.
Checksum: 678660EA24A7E85D

FASTA65871,897
        10         20         30         40         50         60 
MSETLENLLQ ETRTFPPPPE FASRANGTAE LYEKADADHE GFWAEQARTY VSWSKDFTQT 

        70         80         90        100        110        120 
LQWDTPFAKW FPDGELNACY NAVDRHVEAG NGDRVAIHWI GEPEGDTREI TYSDLHSSVQ 

       130        140        150        160        170        180 
RAANALQDIG VRKGDTVAIY LPMIPEAAVA MLACARIGAP HSVVFGGFSA EALHSRIDDA 

       190        200        210        220        230        240 
GAKVVITSDG GYRRGSASPL KPAVDAALDH GDTSVEKVLV VKRTGQETPW TEGRDLWWDE 

       250        260        270        280        290        300 
VLEQAAPTHE APAHESEHPL FILYTSGTTG KPKGIFHTTG GYLTQCAYTN AVVHDVHPES 

       310        320        330        340        350        360 
DVYWCTADIG WVTGHSYIVY GPLTLGATQV MYEGTPDTPH QGRFWEIVEQ KKVTILYTAP 

       370        380        390        400        410        420 
TAIRTFMKWG DDIPGKFDLS SLRLLGSVGE PINPEAWMWY RRVIGGDRCP IVDTWWQTET 

       430        440        450        460        470        480 
GAIMVSPLPG VTATKPGSAQ RAIPGIGAEV VDDMAQPVPN GHGGYLVLTK PWPAMLRGIW 

       490        500        510        520        530        540 
GDPERYKETY WSRFEGLYFA GDGAKKDDDG DIWLLGRVDD VMNVSGHRLS TTEIESALVS 

       550        560        570        580        590        600 
HPKVAEAAVV GATDETTGQA VVAFVILRSE AVAEADEPGE GADIVAELRN HVAKEIGPIA 

       610        620        630        640        650 
KPRSIMIVPE LPKTRSGKIM RRLLRDVAEN RQVGDVTTLA DSSVMELIKT GLNKGDGD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002343 Genomic DNA. Translation: ADU47061.1.
RefSeqYP_004097788.1. NC_014830.1.

3D structure databases

ProteinModelPortalE6S985.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADU47061; ADU47061; Intca_0516.
GeneID10083310.
KEGGica:Intca_0516.
PATRIC45242428. VBIIntCal153415_0517.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000229981.
KOK01895.

Enzyme and pathway databases

BioCycICAL710696:GH9U-529-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 nameE6S985_INTC7
AccessionPrimary (citable) accession number: E6S985
Entry history
Integrated into UniProtKB/TrEMBL: March 8, 2011
Last sequence update: March 8, 2011
Last modified: June 11, 2014
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)