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.

E1RZ77

- E1RZ77_ECOUM

UniProt

E1RZ77 - E1RZ77_ECOUM

(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, UM146_20540
Organism
Escherichia coli (strain UM146)
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. 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 annotationImported

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciECOL869729:GI9Z-4103-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 annotation
Ordered Locus Names:UM146_20540Imported
OrganismiEscherichia coli (strain UM146)Imported
Taxonomic identifieri869729 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000006682: 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

ProteinModelPortaliE1RZ77.
SMRiE1RZ77. Positions 5-647.

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

HOGENOMiHOG000229981.
KOiK01895.
OMAiAWIWYRD.

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.

E1RZ77-1 [UniParc]FASTAAdd to Basket

« Hide

MSQIHKHTIP ANIADRCLIN PQQYEAMYQQ SINAPDTFWG EQGKILDWIT    50
PYQKVKNTSF APGNVSIKWY EDGTLNLAAN CLDRHLQENG DRTAIIWEGD 100
DASQSKHISY KELHRDVCRF ANTLLELGIK KGDVVAIYMP MVPEAAVAML 150
ACARIGAVHS VIFGGFSPEA VAGRIIDSSS RLVITSDEGV RAGRSIPLKK 200
NVDDALKNPN VTSVEHVVVL KRTGGKIDWQ EGRDLWWHDL VEQASDQHQA 250
EEMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAALTFK YVFDYHPGDI 300
YWCTADVGWV TGHSYLLYGP LACGATTLMF EGVPNWPTPA RMAQVVDKHQ 350
VNILYTAPTA IRALMAEGDK AIEGTDRSSL RILGSVGEPI NPEAWEWYWK 400
KIGNEKCPVV DTWWQTETGG FMITPLPGAT ELKAGSATRP FFGVQPALVD 450
NEGNPLEGAT EGSLVITDSW PGQARTLFGD HERFEQTYFS TFKNMYFSGD 500
GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP KIAEAAVVGI 550
PHNIKGQAIY AYVTLNHGEE PSPELYAEVR NWVRKEIGPL ATPDVLHWTD 600
SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVEK LLEEKQAIAM 650
PS 652
Length:652
Mass (Da):72,011
Last modified:November 30, 2010 - v1
Checksum:i3332DC71328CE507
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002167 Genomic DNA. Translation: ADN73438.1.
RefSeqiYP_006112950.1. NC_017632.1.

Genome annotation databases

EnsemblBacteriaiADN73438; ADN73438; UM146_20540.
GeneIDi12702614.
KEGGielu:UM146_20540.
PATRICi42975248. VBIEscCol167775_4412.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002167 Genomic DNA. Translation: ADN73438.1 .
RefSeqi YP_006112950.1. NC_017632.1.

3D structure databases

ProteinModelPortali E1RZ77.
SMRi E1RZ77. Positions 5-647.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADN73438 ; ADN73438 ; UM146_20540 .
GeneIDi 12702614.
KEGGi elu:UM146_20540.
PATRICi 42975248. VBIEscCol167775_4412.

Phylogenomic databases

HOGENOMi HOG000229981.
KOi K01895.
OMAi AWIWYRD.

Enzyme and pathway databases

BioCyci ECOL869729:GI9Z-4103-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

« Hide 'large scale' publications
  1. "Complete genome sequence of adherent invasive Escherichia coli UM146 isolated from ileal Crohn's disease biopsy tissue."
    Krause D.O., Little A.C., Dowd S.E., Bernstein C.N.
    J. Bacteriol. 193:583-583(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: UM146Imported.
  2. "Complete genome sequence of adherent invasive Escherichia coli UM146 isolated from ileal Crohn's disease biopsy tissue."
    Krause D.O., Little A.C., Dowd S.E., Bernstein C.N.
    Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: UM146.

Entry informationi

Entry nameiE1RZ77_ECOUM
AccessioniPrimary (citable) accession number: E1RZ77
Entry historyi
Integrated into UniProtKB/TrEMBL: November 30, 2010
Last sequence update: November 30, 2010
Last modified: June 11, 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 proteome

External Data

Dasty 3

Similar proteinsi