SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

E3DHF3

- E3DHF3_ERWSE

UniProt

E3DHF3 - E3DHF3_ERWSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Acetyl-coenzyme A synthetase
Gene
acs, EJP617_07610
Organism
Erwinia sp. (strain Ejp617)
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. Acs undergoes a two-step reaction. In the first half reaction, Acs 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
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
Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Magnesium By similarity.UniRule annotationSAAS annotations

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei311 – 3111Coenzyme A By similarityUniRule annotation
Binding sitei335 – 3351Coenzyme A By similarityUniRule annotation
Binding sitei387 – 3871Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei500 – 5001Substrate By similarityUniRule annotation
Binding sitei515 – 5151Substrate By similarityUniRule annotation
Active sitei517 – 5171 By similarityUniRule annotation
Binding sitei523 – 5231Coenzyme A By similarityUniRule annotation
Binding sitei526 – 5261Substrate By similarityUniRule annotation
Metal bindingi537 – 5371Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi539 – 5391Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi542 – 5421Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei584 – 5841Coenzyme A By similarityUniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. acetyl-CoA biosynthetic process from acetate Source: UniProtKB-HAMAP
  2. chemotaxis Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotation

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciESP215689:GLCY-773-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:acsUniRule annotationImported
Ordered Locus Names:EJP617_07610Imported
OrganismiErwinia sp. (strain Ejp617)Imported
Taxonomic identifieri215689 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeErwinia
ProteomesiUP000006865: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei609 – 6091N6-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

ProteinModelPortaliE3DHF3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni191 – 1944Coenzyme A By similarityUniRule annotation
Regioni411 – 4166Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

KOiK01895.

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.

E3DHF3-1 [UniParc]FASTAAdd to Basket

« Hide

MSHAHIYPIP ANIAQNTLIN PRQYHSMYQQ SVQDPEAFWG EQGKIVDWIK    50
PYATVKNTSF APGNISIRWY EDGTLNLAAN CLDRHLAARG DHPAMIWEGD 100
DASESKTITY RELHHDVCRF SNALKALGIH KGDVVAIYMP MVPEAAVAML 150
ACARIGAVHS VIFGGFSPEA VAGRIIDSHA RLVITADEGV RAGRTIPLKK 200
NVDDALNNPG VTSVDNVIVL RRTGKEISWH HGRDLWWHEQ VNSASEQHQP 250
EEMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAATTFK YVFDYHPEDI 300
YWCTADVGWI TGHSYLLYGP LACGATTLMF EGVPNWPKPS RMAEVVDKHR 350
VTILYTAPTA VRALMAEGDK AIAGTHRSSL RILGSVGEPI NPEAWEWFHQ 400
KIGNGHCPIS DTWWQTETGG FMIAPLPGAT ALKPGSATHP FFGVQPALVD 450
NEGHLQEGAS EGNLVIVDSW PGQARTLFGD HQRFEQTYFS TFKNRYFSGD 500
GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVSHP KIAEAAVVGI 550
PHALKGQAIY AYITLNRGEE PSPQLYSEVR AWVRKEIGPI ATPDVLHWTE 600
SLPKTRSGKI MRRILRKIAT GDTSNLGDTS TLADPGVVDK LLEEKLSINM 650
P 651
Length:651
Mass (Da):71,837
Last modified:January 11, 2011 - v1
Checksum:iC60FB21842232F2D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002124 Genomic DNA. Translation: ADP10442.1.
RefSeqiWP_014542524.1. NC_017445.1.
YP_005817329.1. NC_017445.1.

Genome annotation databases

EnsemblBacteriaiADP10442; ADP10442; EJP617_07610.
GeneIDi12428730.
KEGGierj:EJP617_07610.
PATRICi42938204. VBIErwSp41759_0819.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002124 Genomic DNA. Translation: ADP10442.1 .
RefSeqi WP_014542524.1. NC_017445.1.
YP_005817329.1. NC_017445.1.

3D structure databases

ProteinModelPortali E3DHF3.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADP10442 ; ADP10442 ; EJP617_07610 .
GeneIDi 12428730.
KEGGi erj:EJP617_07610.
PATRICi 42938204. VBIErwSp41759_0819.

Phylogenomic databases

KOi K01895.

Enzyme and pathway databases

BioCyci ESP215689:GLCY-773-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. "Complete genome sequence of Japanese Erwinia strain Ejp617, a bacterial shoot blight pathogen of pear."
    Park D.H., Thapa S.P., Choi B.S., Kim W.S., Hur J.H., Cho J.M., Lim J.S., Choi I.Y., Lim C.K.
    J. Bacteriol. 193:586-587(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ejp617Imported.

Entry informationi

Entry nameiE3DHF3_ERWSE
AccessioniPrimary (citable) accession number: E3DHF3
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

Similar proteinsi