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E3IPI9

- E3IPI9_DESVR

UniProt

E3IPI9 - E3IPI9_DESVR

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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

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.UniRule annotation

Catalytic activityi

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

Cofactori

Magnesium.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei321 – 3211Coenzyme AUniRule annotation
Binding sitei510 – 5101ATPUniRule annotation
Binding sitei525 – 5251ATPUniRule annotation
Binding sitei533 – 5331Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei536 – 5361ATPUniRule annotation
Metal bindingi547 – 5471Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi549 – 5491Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi552 – 5521Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei594 – 5941Coenzyme AUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi397 – 3993ATPUniRule annotation
Nucleotide bindingi421 – 4266ATPUniRule 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 ligaseUniRule annotation
Acyl-activating enzymeUniRule annotation
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-acetyllysineUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliE3IPI9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni201 – 2044Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

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

        10         20         30         40         50
MSQERIESMM DEKRHFAPPA DSRGRAHVSG EAAREALVRR AAEDPEGFWG
60 70 80 90 100
ERAAQLIDWF KPWDTVLDAD MNEPRIEWFK GGRLNVAHNC LDRHVAGNRR
110 120 130 140 150
NKAAIIWQGE PEEDVRVLTY QMLYDEVRRF AAVLRKMGVH KGDRVSLYMP
160 170 180 190 200
MIPELAVAML ACARIGAVHS IVFAGFSAVS LQNRIHDCEA KVVVTADAVL
210 220 230 240 250
RAGRRIPLKV NVDEAVRQCP SVEKVVVVNR GSLEVTMEEG RDLWWHEVMA
260 270 280 290 300
DRTLDVDRPC EEMDAEDMLF ILYTSGSTGK PKGVVHTTGG YLTYAAHTTQ
310 320 330 340 350
WVFDVQDDDV YWCTADIGWI TGHSYIVYGP LALGATSLMF EGVPSWPSPD
360 370 380 390 400
RFWRIVEKFR VNIFYTAPTV VRALMREGTD WTERHDLSSL RVLGSVGEPI
410 420 430 440 450
NPEAWMWYHT HIGKGRLPIV DTWWQTETGG IMISGLPYAT TLKPGSATQP
460 470 480 490 500
LPGVDAAIVR PDGSPAGPNE GGHLVIRKPW PGMLRGIFGS PERYRSTYFE
510 520 530 540 550
RFPGMYESGD GARTDTDGYF WIMGRLDDVI NVSGHRMGTA EVESALVAHP
560 570 580 590 600
SVAEAAVVGM PHAVKGEAIY AYVTLGADAE ETEELRAELR AWVRKEIGPI
610 620 630 640 650
ATPDVLQFAE GLPKTRSGKI MRRILRKIAA GATSEFGDTS TLADPGVVSD
660
LIEGRLQLTG R
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: October 29, 2014
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3