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E7B6B6

- E7B6B6_YERE1

UniProt

E7B6B6 - E7B6B6_YERE1

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Protein
Acetyl-coenzyme A synthetase
Gene
acs, Y11_35151
Organism
Yersinia enterocolitica subsp. palearctica serotype O:3 (strain DSM 13030 / CIP 106945 / Y11)
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 sitei312 – 3121Coenzyme A By similarityUniRule annotation
Binding sitei336 – 3361Coenzyme A By similarityUniRule annotation
Binding sitei388 – 3881Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei501 – 5011Substrate By similarityUniRule annotation
Binding sitei516 – 5161Substrate By similarityUniRule annotation
Active sitei518 – 5181 By similarityUniRule annotation
Binding sitei524 – 5241Coenzyme A By similarityUniRule annotation
Binding sitei527 – 5271Substrate By similarityUniRule annotation
Metal bindingi538 – 5381Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi540 – 5401Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi543 – 5431Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei585 – 5851Coenzyme 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 annotationImported

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciYENT930944:GLMU-3592-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:Y11_35151Imported
OrganismiYersinia enterocolitica subsp. palearctica serotype O:3 (strain DSM 13030 / CIP 106945 / Y11)Imported
Taxonomic identifieri930944 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000008084: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei610 – 6101N6-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

ProteinModelPortaliE7B6B6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni192 – 1954Coenzyme A By similarityUniRule annotation
Regioni412 – 4176Substrate 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.

E7B6B6-1 [UniParc]FASTAAdd to Basket

« Hide

MMSQIHKHPI PTAIAEHALI NPEQYHQYYQ QSVQNPDEFW GEHGKIIDWI    50
KPYKTVKNTS FDPGHVSIRW FEDGTLNLAA NCLDRHLAER SDQTAIIWEG 100
DDPNQSKTVT YKQLHHDVCQ FANVLKKLGI KKGDVVAIYM PMVPEAAVAM 150
LACARIGAVH SVIFGGFSPD AVAGRIIDSN SKLVITADEG IRAGRAIPLK 200
KNVDEALKNP AITSIKNVVV FQRTGNASYW KDGRDVWWHD LIENASADCP 250
PEEMNAEDPL FILYTSGSTG KPKGVLHTTG GYLVYAALTF KYVFDYHPGD 300
IYWCTADVGW VTGHSYLLYG PLACGAITLM FEGVPNYPGV NRLGQVIDKH 350
QVNILYTAPT AIRALMAEGD KAIEDTKRTS LRIMGSVGEP INPEAWEWYY 400
NKIGNSKCPI VDTWWQTETG GFMITPLPGA TELKAGSATR PFFGVQPALV 450
DNLGNPQEGA AEGNLVITDS WPGQARTLFG DHDRFEQTYF STFKGMYFSG 500
DGARRDEDGY YWITGRVDDV LNVSGHRLGT AEIESALVSH PKIAEAAVVG 550
VPHNIKGQAI YAYITLNHGE EPTPELYTEV RNWVRKEIGP IATPDILHWT 600
DSLPKTRSGK IMRRILRKIA AGDTSNLGDT STLADPGVVD KLLEEKQSMQ 650
APS 653
Length:653
Mass (Da):72,214
Last modified:March 8, 2011 - v1
Checksum:i07271790E643740E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FR729477 Genomic DNA. Translation: CBY29015.1.
RefSeqiYP_006007014.1. NC_017564.1.

Genome annotation databases

EnsemblBacteriaiCBY29015; CBY29015; Y11_35151.
GeneIDi12602229.
KEGGiyey:Y11_35151.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FR729477 Genomic DNA. Translation: CBY29015.1 .
RefSeqi YP_006007014.1. NC_017564.1.

3D structure databases

ProteinModelPortali E7B6B6.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CBY29015 ; CBY29015 ; Y11_35151 .
GeneIDi 12602229.
KEGGi yey:Y11_35151.

Phylogenomic databases

KOi K01895.

Enzyme and pathway databases

BioCyci YENT930944:GLMU-3592-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 Y. enterocolitica subsp. palearctica serogroup O:3."
    Batzilla J., Hoeper D., Heesemann J., Rakin A.
    Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Y11.
  2. "Complete genome sequence of Yersinia enterocolitica subsp. palearctica serogroup O:3."
    Batzilla J., Hoper D., Antonenka U., Heesemann J., Rakin A.
    J. Bacteriol. 193:2067-2067(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 13030 / CIP 106945 / Y11.

Entry informationi

Entry nameiE7B6B6_YERE1
AccessioniPrimary (citable) accession number: E7B6B6
Entry historyi
Integrated into UniProtKB/TrEMBL: March 8, 2011
Last sequence update: March 8, 2011
Last modified: June 11, 2014
This is version 22 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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