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E3IPI9

- E3IPI9_DESVR

UniProt

E3IPI9 - E3IPI9_DESVR

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Protein

Acetyl-coenzyme A synthetase

Gene
acsA, Deval_2742
Organism
Desulfovibrio vulgaris (strain RCH1)
Status
Unreviewed - 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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Magnesium By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei321 – 3211Coenzyme A By similarityUniRule annotation
Binding sitei397 – 3971Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei510 – 5101Substrate By similarityUniRule annotation
Binding sitei525 – 5251Substrate By similarityUniRule annotation
Active sitei527 – 5271 By similarityUniRule annotation
Binding sitei533 – 5331Coenzyme A By similarityUniRule annotation
Binding sitei536 – 5361Substrate By similarityUniRule annotation
Metal bindingi547 – 5471Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi549 – 5491Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi552 – 5521Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei594 – 5941Coenzyme A By similarityUniRule annotation

GO - Molecular functioni

  1. acetate-CoA ligase activity Source: UniProtKB-HAMAP
  2. AMP binding Source: InterPro
  3. ATP binding Source: UniProtKB-KW
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. acetyl-CoA biosynthetic process from acetate Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotationImported

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciDVUL573059:GLCM-2818-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 ligase
Acyl-activating enzyme
Gene namesi
Name:acsAUniRule annotation
Ordered Locus Names:Deval_2742Imported
OrganismiDesulfovibrio vulgaris (strain RCH1)Imported
Taxonomic identifieri573059 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
ProteomesiUP000001496: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei619 – 6191N6-acetyllysine By similarityUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliE3IPI9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni201 – 2044Coenzyme A By similarityUniRule annotation
Regioni421 – 4266Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

KOiK01895.
OMAiRRIFEPT.

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.

E3IPI9-1 [UniParc]FASTAAdd to Basket

« Hide

MSQERIESMM DEKRHFAPPA DSRGRAHVSG EAAREALVRR AAEDPEGFWG    50
ERAAQLIDWF KPWDTVLDAD MNEPRIEWFK GGRLNVAHNC LDRHVAGNRR 100
NKAAIIWQGE PEEDVRVLTY QMLYDEVRRF AAVLRKMGVH KGDRVSLYMP 150
MIPELAVAML ACARIGAVHS IVFAGFSAVS LQNRIHDCEA KVVVTADAVL 200
RAGRRIPLKV NVDEAVRQCP SVEKVVVVNR GSLEVTMEEG RDLWWHEVMA 250
DRTLDVDRPC EEMDAEDMLF ILYTSGSTGK PKGVVHTTGG YLTYAAHTTQ 300
WVFDVQDDDV YWCTADIGWI TGHSYIVYGP LALGATSLMF EGVPSWPSPD 350
RFWRIVEKFR VNIFYTAPTV VRALMREGTD WTERHDLSSL RVLGSVGEPI 400
NPEAWMWYHT HIGKGRLPIV DTWWQTETGG IMISGLPYAT TLKPGSATQP 450
LPGVDAAIVR PDGSPAGPNE GGHLVIRKPW PGMLRGIFGS PERYRSTYFE 500
RFPGMYESGD GARTDTDGYF WIMGRLDDVI NVSGHRMGTA EVESALVAHP 550
SVAEAAVVGM PHAVKGEAIY AYVTLGADAE ETEELRAELR AWVRKEIGPI 600
ATPDVLQFAE GLPKTRSGKI MRRILRKIAA GATSEFGDTS TLADPGVVSD 650
LIEGRLQLTG R 661
Length:661
Mass (Da):73,499
Last modified:January 11, 2011 - v1
Checksum:iD33CE2558CB40921
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002297 Genomic DNA. Translation: ADP87884.1.
RefSeqiWP_010940228.1. NC_017310.1.
YP_005703522.1. NC_017310.1.

Genome annotation databases

EnsemblBacteriaiADP87884; ADP87884; Deval_2742.
GeneIDi12868602.
KEGGidvg:Deval_2742.
PATRICi42913287. VBIDesVul75230_2905.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002297 Genomic DNA. Translation: ADP87884.1 .
RefSeqi WP_010940228.1. NC_017310.1.
YP_005703522.1. NC_017310.1.

3D structure databases

ProteinModelPortali E3IPI9.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADP87884 ; ADP87884 ; Deval_2742 .
GeneIDi 12868602.
KEGGi dvg:Deval_2742.
PATRICi 42913287. VBIDesVul75230_2905.

Phylogenomic databases

KOi K01895.
OMAi RRIFEPT.

Enzyme and pathway databases

BioCyci DVUL573059:GLCM-2818-MONOMER.

Family and domain databases

HAMAPi MF_01123. Ac_CoA_synth.
InterProi IPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RCH1Imported.

Entry informationi

Entry nameiE3IPI9_DESVR
AccessioniPrimary (citable) accession number: E3IPI9
Entry historyi
Integrated into UniProtKB/TrEMBL: January 11, 2011
Last sequence update: January 11, 2011
Last modified: September 3, 2014
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

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