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E7B6B6 (E7B6B6_YERE1) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123

Short name=AcCoA synthetase HAMAP-Rule MF_01123
Short name=Acs HAMAP-Rule MF_01123
EC=6.2.1.1 HAMAP-Rule MF_01123
Alternative name(s):
Acetate--CoA ligase HAMAP-Rule MF_01123
Acyl-activating enzyme HAMAP-Rule MF_01123
Gene names
Name:acs HAMAP-Rule MF_01123
Ordered Locus Names:Y11_35151 EMBL CBY29015.1
OrganismYersinia enterocolitica subsp. palearctica serotype O:3 (strain DSM 13030 / CIP 106945 / Y11) [Complete proteome] [HAMAP] EMBL CBY29015.1
Taxonomic identifier930944 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length653 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_01123

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. HAMAP-Rule MF_01123

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. HAMAP-Rule MF_01123

Catalytic activity

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP-Rule MF_01123

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01123 SAAS SAAS020845

Post-translational modification

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity. HAMAP-Rule MF_01123

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family. HAMAP-Rule MF_01123

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region192 – 1954Coenzyme A By similarity HAMAP-Rule MF_01123
Region412 – 4176Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5181 By similarity HAMAP-Rule MF_01123
Metal binding5381Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5401Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5431Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3121Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3361Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3881Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5011Substrate By similarity HAMAP-Rule MF_01123
Binding site5161Substrate By similarity HAMAP-Rule MF_01123
Binding site5241Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5271Substrate By similarity HAMAP-Rule MF_01123
Binding site5851Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6101N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
E7B6B6 [UniParc].

Last modified March 8, 2011. Version 1.
Checksum: 07271790E643740E

FASTA65372,214
        10         20         30         40         50         60 
MMSQIHKHPI PTAIAEHALI NPEQYHQYYQ QSVQNPDEFW GEHGKIIDWI KPYKTVKNTS 

        70         80         90        100        110        120 
FDPGHVSIRW FEDGTLNLAA NCLDRHLAER SDQTAIIWEG DDPNQSKTVT YKQLHHDVCQ 

       130        140        150        160        170        180 
FANVLKKLGI KKGDVVAIYM PMVPEAAVAM LACARIGAVH SVIFGGFSPD AVAGRIIDSN 

       190        200        210        220        230        240 
SKLVITADEG IRAGRAIPLK KNVDEALKNP AITSIKNVVV FQRTGNASYW KDGRDVWWHD 

       250        260        270        280        290        300 
LIENASADCP PEEMNAEDPL FILYTSGSTG KPKGVLHTTG GYLVYAALTF KYVFDYHPGD 

       310        320        330        340        350        360 
IYWCTADVGW VTGHSYLLYG PLACGAITLM FEGVPNYPGV NRLGQVIDKH QVNILYTAPT 

       370        380        390        400        410        420 
AIRALMAEGD KAIEDTKRTS LRIMGSVGEP INPEAWEWYY NKIGNSKCPI VDTWWQTETG 

       430        440        450        460        470        480 
GFMITPLPGA TELKAGSATR PFFGVQPALV DNLGNPQEGA AEGNLVITDS WPGQARTLFG 

       490        500        510        520        530        540 
DHDRFEQTYF STFKGMYFSG DGARRDEDGY YWITGRVDDV LNVSGHRLGT AEIESALVSH 

       550        560        570        580        590        600 
PKIAEAAVVG VPHNIKGQAI YAYITLNHGE EPTPELYTEV RNWVRKEIGP IATPDILHWT 

       610        620        630        640        650 
DSLPKTRSGK IMRRILRKIA AGDTSNLGDT STLADPGVVD KLLEEKQSMQ APS 

« Hide

References

« Hide 'large scale' references
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FR729477 Genomic DNA. Translation: CBY29015.1.
RefSeqYP_006007014.1. NC_017564.1.

3D structure databases

ProteinModelPortalE7B6B6.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCBY29015; CBY29015; Y11_35151.
GeneID12602229.
KEGGyey:Y11_35151.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01895.

Enzyme and pathway databases

BioCycYENT930944:GLMU-3592-MONOMER.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
InterProIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE7B6B6_YERE1
AccessionPrimary (citable) accession number: E7B6B6
Entry history
Integrated into UniProtKB/TrEMBL: March 8, 2011
Last sequence update: March 8, 2011
Last modified: February 19, 2014
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)