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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Kitasatospora setae (strain ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 / KM-6054) (Streptomyces setae)
Status
Unreviewed-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

LigaseUniRule annotationImported

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotation, Metal-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

BioCyciKSET452652:GJFD-3594-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 annotationImported
Ordered Locus Names:KSE_35980Imported
OrganismiKitasatospora setae (strain ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 / KM-6054) (Streptomyces setae)Imported
Taxonomic identifieri452652 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeKitasatospora
ProteomesiUP000007076 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei610 – 6101N6-acetyllysineUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi452652.KSE_35980.

Structurei

3D structure databases

ProteinModelPortaliE4NDX1.
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

KOiK01895.
OMAiPMDSEDM.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
InterProiIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. 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.

E4NDX1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNESLANLL KEERRFAPPA ELAASANVTA DAYAQASEDR LAFWAEQARR
60 70 80 90 100
LSWAVEPTET LDWSNPPFAK WFADGKLNVA YNCVDRHVEA GNGDRVAIHF
110 120 130 140 150
EGEPGDSRAI TYAQLKDEVS KAANALESLG VAKGDRVAVY LPMIPEAVVA
160 170 180 190 200
MLACARIGAA HSVVFGGFSA DAVASRIKDA DAKLVITADG GYRRGKPSAL
210 220 230 240 250
KPAIDEALTK VDGVENVLVV RRTGEEVAWT EGRDVWWHEL VDGQSAEHTP
260 270 280 290 300
EAHDAEQPLF ILYTSGTTGK PKGILHTSGG YLTQASFTHN AVFDLKPETD
310 320 330 340 350
VYWCTADIGW VTGHSYIVYG PLSNGATQVI YEGTPDTPHQ GRMFEIVQKY
360 370 380 390 400
GVTILYTAPT LIRTWMKWGD DIPAGFDLSS LRVLGSVGEP INPEAWVWYR
410 420 430 440 450
EHIGAGKTPI VDTWWQTETG AIMISPLPGV TETKPGSAQR ALPGIAATVV
460 470 480 490 500
DDEAREVPNG SGGYLVLTEP WPSMLRTIWG DDERYVDTYW SRFEGRYFAG
510 520 530 540 550
DGAKKDEDGD IWLLGRVDDV MLVSGHNIST TEVESALVGH PAVAESAVVG
560 570 580 590 600
AADATTGQAI VAFVILRGTA ADSEELIADL RNHVGKTLGP IAKPKQIKVV
610 620 630 640 650
SELPKTRSGK IMRRLLRDIA EGREVGDTTT LADSSVMNLI QSQLPAAGAE

G
Length:651
Mass (Da):70,350
Last modified:February 8, 2011 - v1
Checksum:i227EFC38369A670D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP010968 Genomic DNA. Translation: BAJ29402.1.

Genome annotation databases

EnsemblBacteriaiBAJ29402; BAJ29402; KSE_35980.
KEGGiksk:KSE_35980.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP010968 Genomic DNA. Translation: BAJ29402.1.

3D structure databases

ProteinModelPortaliE4NDX1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi452652.KSE_35980.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAJ29402; BAJ29402; KSE_35980.
KEGGiksk:KSE_35980.

Phylogenomic databases

KOiK01895.
OMAiPMDSEDM.

Enzyme and pathway databases

BioCyciKSET452652:GJFD-3594-MONOMER.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
InterProiIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 / KM-6054Imported.

Entry informationi

Entry nameiE4NDX1_KITSK
AccessioniPrimary (citable) accession number: E4NDX1
Entry historyi
Integrated into UniProtKB/TrEMBL: February 8, 2011
Last sequence update: February 8, 2011
Last modified: July 22, 2015
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.