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E3DHF3

- E3DHF3_ERWSE

UniProt

E3DHF3 - E3DHF3_ERWSE

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Protein

Acetyl-coenzyme A synthetase

Gene

acs

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.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.UniRule annotation

Catalytic activityi

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

Cofactori

Note: Magnesium.UniRule annotationSAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei311 – 3111Coenzyme AUniRule annotation
Binding sitei335 – 3351Coenzyme AUniRule annotation
Binding sitei500 – 5001ATPUniRule annotation
Binding sitei515 – 5151ATPUniRule annotation
Binding sitei523 – 5231Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei526 – 5261ATPUniRule annotation
Metal bindingi537 – 5371Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi539 – 5391Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi542 – 5421Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei584 – 5841Coenzyme AUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi387 – 3893ATPUniRule annotation
Nucleotide bindingi411 – 4166ATPUniRule 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: UniProtKB-HAMAP
  2. chemotaxis Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotation

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation, 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 ligaseUniRule annotation
Acyl-activating enzymeUniRule annotation
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-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

ProteinModelPortaliE3DHF3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni191 – 1944Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

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

        10         20         30         40         50
MSHAHIYPIP ANIAQNTLIN PRQYHSMYQQ SVQDPEAFWG EQGKIVDWIK
60 70 80 90 100
PYATVKNTSF APGNISIRWY EDGTLNLAAN CLDRHLAARG DHPAMIWEGD
110 120 130 140 150
DASESKTITY RELHHDVCRF SNALKALGIH KGDVVAIYMP MVPEAAVAML
160 170 180 190 200
ACARIGAVHS VIFGGFSPEA VAGRIIDSHA RLVITADEGV RAGRTIPLKK
210 220 230 240 250
NVDDALNNPG VTSVDNVIVL RRTGKEISWH HGRDLWWHEQ VNSASEQHQP
260 270 280 290 300
EEMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAATTFK YVFDYHPEDI
310 320 330 340 350
YWCTADVGWI TGHSYLLYGP LACGATTLMF EGVPNWPKPS RMAEVVDKHR
360 370 380 390 400
VTILYTAPTA VRALMAEGDK AIAGTHRSSL RILGSVGEPI NPEAWEWFHQ
410 420 430 440 450
KIGNGHCPIS DTWWQTETGG FMIAPLPGAT ALKPGSATHP FFGVQPALVD
460 470 480 490 500
NEGHLQEGAS EGNLVIVDSW PGQARTLFGD HQRFEQTYFS TFKNRYFSGD
510 520 530 540 550
GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVSHP KIAEAAVVGI
560 570 580 590 600
PHALKGQAIY AYITLNRGEE PSPQLYSEVR AWVRKEIGPI ATPDVLHWTE
610 620 630 640 650
SLPKTRSGKI MRRILRKIAT GDTSNLGDTS TLADPGVVDK LLEEKLSINM

P
Length:651
Mass (Da):71,837
Last modified:January 11, 2011 - v1
Checksum:iC60FB21842232F2D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 27 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