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I0A418

- I0A418_SALET

UniProt

I0A418 - I0A418_SALET

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Protein

Acetyl-coenzyme A synthetase

Gene
acs, SU5_0348
Organism
Salmonella enterica subsp. enterica serovar Heidelberg str. B182
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

BioCyciSENT1160717:GLJS-389-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
ORF Names:SU5_0348Imported
OrganismiSalmonella enterica subsp. enterica serovar Heidelberg str. B182Imported
Taxonomic identifieri1160717 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000007393: 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

ProteinModelPortaliI0A418.

Family & Domainsi

Region

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

Sequence similaritiesi

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.

I0A418-1 [UniParc]FASTAAdd to Basket

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MSQTHKHAIP ANIADRCLIN PEQYETKYKQ SINDPDTFWG EQGKILDWIT    50
PYQKVKNTSF APGNVSIKWY EDGTLNLAAN CLDRHLQENG DRTAIIWEGD 100
DASQSKHISY RELHRDVCRF ANTLLDLGIK KGDVVAIYMP MVPEAAVAML 150
ACARIGAVHS VIFGGFSPEA VAGRIIDSSS RLVITADEGV RAGRSIPLKK 200
NVDDALKNPN VTSVEHVIVL KRTGSDIDWQ EGRDLWWRDL IEKASPEHQP 250
EAMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAATTFK YVFDYHPGDI 300
YWCTADVGWV TGHSYLLYGP LACGATTLMF EGVPNWPTPA RMCQVVDKHQ 350
VNILYTAPTA IRALMAEGDK AIEGTDRSSL RILGSVGEPI NPEAWEWYWK 400
KIGKEKCPVV DTWWQTETGG FMITPLPGAI ELKAGSATRP FFGVQPALVD 450
NEGHPQEGAT EGNLVITDSW PGQARTLFGD HERFEQTYFS TFKNMYFSGD 500
GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP KIAEAAVVGI 550
PHAIKGQAIY AYVTLNHGEE PSPELYAEVR NWVRKEIGPL ATPDVLHWTD 600
SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVEK LLEEKQAIAM 650
PS 652
Length:652
Mass (Da):72,123
Last modified:June 13, 2012 - v1
Checksum:iD575C4A0D3D34C17
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003416 Genomic DNA. Translation: AFH43725.1.
RefSeqiYP_006085999.1. NC_017623.1.

Genome annotation databases

EnsemblBacteriaiAFH43725; AFH43725; SU5_0348.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003416 Genomic DNA. Translation: AFH43725.1 .
RefSeqi YP_006085999.1. NC_017623.1.

3D structure databases

ProteinModelPortali I0A418.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AFH43725 ; AFH43725 ; SU5_0348 .

Enzyme and pathway databases

BioCyci SENT1160717:GLJS-389-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 the Strong Mutator Salmonella enterica subsp. enterica Serotype Heidelberg Strain B182."
    Le Bars H., Bousarghin L., Bonnaure-Mallet M., Jolivet-Gougeon A., Barloy-Hubler F.
    J. Bacteriol. 194:3537-3538(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B182Imported.

Entry informationi

Entry nameiI0A418_SALET
AccessioniPrimary (citable) accession number: I0A418
Entry historyi
Integrated into UniProtKB/TrEMBL: June 13, 2012
Last sequence update: June 13, 2012
Last modified: September 3, 2014
This is version 16 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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