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.

A1JIK3

- ACSA_YERE8

UniProt

A1JIK3 - ACSA_YERE8

(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, YE0309
Organism
Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)
Status
Reviewed - Annotation score: 4 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
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 annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei311 – 3111Coenzyme A By similarity
Binding sitei335 – 3351Coenzyme A By similarity
Binding sitei387 – 3871Substrate; via amide nitrogen By similarity
Binding sitei500 – 5001Substrate By similarity
Binding sitei515 – 5151Substrate By similarity
Active sitei517 – 5171 By similarity
Binding sitei523 – 5231Coenzyme A By similarity
Binding sitei526 – 5261Substrate By similarity
Metal bindingi537 – 5371Magnesium; via carbonyl oxygen By similarity
Metal bindingi539 – 5391Magnesium; via carbonyl oxygen By similarity
Metal bindingi542 – 5421Magnesium; via carbonyl oxygen By similarity
Binding sitei584 – 5841Coenzyme A

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

Ligase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A synthetase (EC:6.2.1.1)
Short name:
AcCoA synthetase
Short name:
Acs
Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme
Gene namesi
Name:acs
Ordered Locus Names:YE0309
OrganismiYersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)
Taxonomic identifieri393305 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000000642: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 652652Acetyl-coenzyme A synthetaseUniRule annotation
PRO_1000065332Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei609 – 6091N6-acetyllysine By similarity

Post-translational modificationi

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity.UniRule annotation

Keywords - PTMi

Acetylation

Interactioni

Protein-protein interaction databases

STRINGi393305.YE0309.

Structurei

3D structure databases

ProteinModelPortaliA1JIK3.
SMRiA1JIK3. Positions 5-647.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiKMEHLRI.
OrthoDBiEOG68WR2H.

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.

A1JIK3-1 [UniParc]FASTAAdd to Basket

« Hide

MSQIHKHPIP TAIAEHALIN PEQYHQYYQQ SVQNPDEFWG EHGKIIDWIK    50
PYKTVKNTSF DPGHVSIRWF EDGTLNLAAN CLDRHLAERG DQTAIIWEGD 100
DPNQSKTVTY KQLHHDVCQF ANVLKKLGIK KGDVVAIYMP MVPEAAVAML 150
ACARIGAVHS VIFGGFSPDA VAGRIIDSNS KLVITADEGI RAGRAIPLKK 200
NVDEALKNPA ITSIKNVVVF QRTGNASYWK DGRDVWWHDL IKDASVDCPP 250
EEMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAALTFK YVFDYHPGDI 300
YWCTADVGWV TGHSYLLYGP LACGAITLMF EGVPNYPGVN RLGQVIDKHQ 350
VNILYTAPTA IRALMAEGDK AIEGTKRTSL RIMGSVGEPI NPEAWEWYYN 400
KIGNSKCPIV DTWWQTETGG FMITPLPGAT ELKAGSATRP FFGVQPALVD 450
NLGNPQEGAA EGNLVITDSW PGQARTLFGD HERFEQTYFS TFKGMYFSGD 500
GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVSHP KIAEAAVVGV 550
PHNIKGQAIY AYITLNHGEE PTPELYTEVR NWVRKEIGPI ATPDILHWTD 600
SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVDK LLEEKQSMQA 650
PS 652
Length:652
Mass (Da):72,037
Last modified:February 6, 2007 - v1
Checksum:i8CE422D75BDFC155
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM286415 Genomic DNA. Translation: CAL10441.1.
RefSeqiYP_001004690.1. NC_008800.1.

Genome annotation databases

EnsemblBacteriaiCAL10441; CAL10441; YE0309.
GeneIDi4714425.
KEGGiyen:YE0309.
PATRICi18560010. VBIYerEnt11519_0402.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM286415 Genomic DNA. Translation: CAL10441.1 .
RefSeqi YP_001004690.1. NC_008800.1.

3D structure databases

ProteinModelPortali A1JIK3.
SMRi A1JIK3. Positions 5-647.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 393305.YE0309.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAL10441 ; CAL10441 ; YE0309 .
GeneIDi 4714425.
KEGGi yen:YE0309.
PATRICi 18560010. VBIYerEnt11519_0402.

Phylogenomic databases

eggNOGi COG0365.
HOGENOMi HOG000229981.
KOi K01895.
OMAi KMEHLRI.
OrthoDBi EOG68WR2H.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NCTC 13174 / 8081.

Entry informationi

Entry nameiACSA_YERE8
AccessioniPrimary (citable) accession number: A1JIK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 6, 2007
Last modified: May 14, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi