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H8J0W5 (H8J0W5_MYCIT) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 8. 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
ORF Names:OCO_04070 EMBL AFC46771.1
OrganismMycobacterium intracellulare MOTT-02 EMBL AFC46771.1
Taxonomic identifier1138382 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium avium complex (MAC) ›

Protein attributes

Sequence length651 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

Region410 – 4156Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5251 By similarity HAMAP-Rule MF_01123
Metal binding5451Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5471Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5501Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3101Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3861Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5081Substrate By similarity HAMAP-Rule MF_01123
Binding site5231Substrate By similarity HAMAP-Rule MF_01123
Binding site5311Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5341Substrate By similarity HAMAP-Rule MF_01123
Binding site5921Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6171N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
H8J0W5 [UniParc].

Last modified May 16, 2012. Version 1.
Checksum: BCA7FF98808D6AC4

FASTA65171,545
        10         20         30         40         50         60 
MTATNSAGPS SYPPSARFAE QANAGEELYR DAERDRLAFW AEQANRLSWA TPFTEVLDWS 

        70         80         90        100        110        120 
DAPFAKWFGD GKLNVAYNCV DRHVEAGHGD RVAIHWEGEP VGDHRSLTYS QLQTEVCKAA 

       130        140        150        160        170        180 
NALTDLGLVA GDRVAIYLPL IPEAVIAMLA CARLGIMHSV VFAGFTAKAL QARIADADAK 

       190        200        210        220        230        240 
LLITSDGQFR RGRPAPLKDA ADEAVSDPDS PIEHVVVVRR TGIDVSWNDD RDLWWHDVVD 

       250        260        270        280        290        300 
AASPEHTPQP FDAEQPLFLL YTSGTTGKPK GIVHTSGGYL THAAYTHYYV FDIKADSDVF 

       310        320        330        340        350        360 
WCTADIGWVT GHTYGVYGPL ANGVTEVLYE GTPDSPSQHR HFEIIEKYGV TIYYTAPTLI 

       370        380        390        400        410        420 
RTFMKWGREV PDAHDLSSLR LLGSVGEPIN PEAWRWYRKV IGADSLPIVD TWWQTETGAT 

       430        440        450        460        470        480 
MISPLPGIAA AKPGSAMRPL PGVSAKIVDD HGEELPPPGE DKGEHVTGYL VLDQPWPSML 

       490        500        510        520        530        540 
RGIWGDPQRY VETYWSRFAE QGWYFAGDSA YYDTEGDIWV VGRIDDVMNV SGHRLSTAEV 

       550        560        570        580        590        600 
ESALVGHAAV AEAAVVGATD ETTGQAICAF VVLCADFEVH DGIVDDLRVE VAREISPIAR 

       610        620        630        640        650 
PREVHVVPEL PKTRSGKIMR RLLRDIAENR ELGDTSTLLD PGVFDAIRAA K

« Hide

References

[1]"Complete Genome Sequence of Mycobacterium intracellulare Clinical Strain MOTT-02."
Kim B.J., Choi B.S., Lim J.S., Choi I.Y., Lee J.H., Chun J., Kook Y.H., Kim B.J.
J. Bacteriol. 194:2771-2771(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: MOTT-02 EMBL AFC46771.1.
[2]Kim B.-J., Lee J.H., Lim J.-S., Choi I.-Y., Choi B.-S., Lim J.-S.
Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: MOTT-02 EMBL AFC46771.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP003323 Genomic DNA. Translation: AFC46771.1.
RefSeqYP_005341092.1. NC_016947.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFC46771; AFC46771; OCO_04070.
GeneID11901923.
KEGGmit:OCO_04070.

Phylogenomic databases

KOK01895.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
InterProIPR011904. Ac_CoA_lig.
IPR024597. Acyl-CoA_synth_DUF3448.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR025110. DUF4009.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF11930. DUF3448. 1 hit.
PF13193. DUF4009. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameH8J0W5_MYCIT
AccessionPrimary (citable) accession number: H8J0W5
Entry history
Integrated into UniProtKB/TrEMBL: May 16, 2012
Last sequence update: May 16, 2012
Last modified: April 3, 2013
This is version 8 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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