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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.UniRule annotation

Cofactori

Mg2+UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei312 – 3121Coenzyme AUniRule annotation
Binding sitei501 – 5011ATPUniRule annotation
Binding sitei516 – 5161ATPUniRule annotation
Binding sitei524 – 5241Coenzyme A; via carbonyl oxygenUniRule annotation
Metal bindingi538 – 5381Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi540 – 5401Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi543 – 5431Magnesium; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi388 – 3903ATPUniRule annotation
Nucleotide bindingi412 – 4176ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciSAVE227882:GJU1-4652-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A synthetaseUniRule annotation (EC:6.2.1.1UniRule annotation)
Short name:
AcCoA synthetaseUniRule annotation
Short name:
AcsUniRule annotation
Alternative name(s):
Acetate--CoA ligaseUniRule annotation
Acyl-activating enzymeUniRule annotation
Gene namesi
Name:acsAUniRule annotation
Ordered Locus Names:SAV_4599
OrganismiStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
Taxonomic identifieri227882 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces
Proteomesi
  • UP000000428 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 652652Acetyl-coenzyme A synthetasePRO_0000208388Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei611 – 6111N6-acetyllysineUniRule annotation

Post-translational modificationi

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.UniRule annotation

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiQ82EL5.

Interactioni

Protein-protein interaction databases

STRINGi227882.SAV_4599.

Structurei

3D structure databases

ProteinModelPortaliQ82EL5.
SMRiQ82EL5. Positions 15-644.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni193 – 1964Coenzyme A bindingUniRule annotation

Sequence similaritiesi

Belongs to the ATP-dependent AMP-binding enzyme family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiPMDSEDM.
OrthoDBiEOG68WR2H.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q82EL5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNESLANLL KEERRFAPPA DLAANANVTA EAYEQAKADR LGFWAEQARR
60 70 80 90 100
LTWATEPTET LDWSNPPFAK WFKDGKLNVA YNCVDRHVEA GHGDRVAIHF
110 120 130 140 150
EGEPGDSRAI TYAELKDEVS KAANALTELG VQKGDRVAVY LPMIPEAVVA
160 170 180 190 200
MLACARIGAA HSVVFGGFSA DAIAARIKDA DAKLVITADG GYRRGKPSAL
210 220 230 240 250
KPAVDDAVSR GDGVEKVLVV RRTGQEVAWT EGRDVWWHEI TAKQSAEHTP
260 270 280 290 300
EAFDAEHPLF ILYTSGTTGK PKGILHTSGG YLTQTSYTHH AVFDLKPETD
310 320 330 340 350
VYWCTADIGW VTGHSYITYG PLSNGATQVM YEGTPDTPHQ GRFWEIVQKY
360 370 380 390 400
GVTILYTAPT AIRTFMKWGD DIPAKFDLSS LRVLGSVGEP INPEAWIWYR
410 420 430 440 450
KHIGGDRTPI VDTWWQTETG AMMISPLPGV TETKPGSAQR PLPGISATVV
460 470 480 490 500
DDEAREVPNG GGGYLVLTEP WPSMLRTIWG DDQRFLDTYW SRFEGKYFAG
510 520 530 540 550
DGAKKDEDGD IWLLGRVDDV MLVSGHNIST TEVESALVSH PSVAEAAVVG
560 570 580 590 600
AADETTGQAI VAFVILRGTA NAEDDNLVAD LRNHVGTTLG PIAKPKRILP
610 620 630 640 650
VAELPKTRSG KIMRRLLRDV AENRALGDVT TLTDSSVMDL IQSKLPAAPS

ED
Length:652
Mass (Da):71,091
Last modified:June 1, 2003 - v1
Checksum:iF9834F4332A3279A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000030 Genomic DNA. Translation: BAC72311.1.
RefSeqiWP_010986023.1. NZ_JZJK01000062.1.

Genome annotation databases

EnsemblBacteriaiBAC72311; BAC72311; SAV_4599.
KEGGisma:SAV_4599.
PATRICi23723073. VBIStrAve112782_4916.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000030 Genomic DNA. Translation: BAC72311.1.
RefSeqiWP_010986023.1. NZ_JZJK01000062.1.

3D structure databases

ProteinModelPortaliQ82EL5.
SMRiQ82EL5. Positions 15-644.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi227882.SAV_4599.

Proteomic databases

PRIDEiQ82EL5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC72311; BAC72311; SAV_4599.
KEGGisma:SAV_4599.
PATRICi23723073. VBIStrAve112782_4916.

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiPMDSEDM.
OrthoDBiEOG68WR2H.

Enzyme and pathway databases

BioCyciSAVE227882:GJU1-4652-MONOMER.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
    Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
    Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680.
  2. "Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
    Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
    Nat. Biotechnol. 21:526-531(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680.

Entry informationi

Entry nameiACSA_STRAW
AccessioniPrimary (citable) accession number: Q82EL5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: June 1, 2003
Last modified: November 11, 2015
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.