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A4TS06

- ACSA_YERPP

UniProt

A4TS06 - ACSA_YERPP

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Protein
Acetyl-coenzyme A synthetase
Gene
acs, YPDSF_3718
Organism
Yersinia pestis (strain Pestoides F)
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

Enzyme and pathway databases

BioCyciYPES386656:GKD7-3806-MONOMER.

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:YPDSF_3718
OrganismiYersinia pestis (strain Pestoides F)
Taxonomic identifieri386656 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000000236: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 652652Acetyl-coenzyme A synthetaseUniRule annotation
PRO_1000065336Add
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

Proteomic databases

PRIDEiA4TS06.

Interactioni

Protein-protein interaction databases

STRINGi386656.YPDSF_3718.

Structurei

3D structure databases

ProteinModelPortaliA4TS06.
SMRiA4TS06. 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.

A4TS06-1 [UniParc]FASTAAdd to Basket

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MSQIHKHPIP AAIAEHALIT PEKYQHYYQQ SVQNPDEFWG EQGKIIDWIK    50
PYKTVKNTSF DPGHVSIRWF EDGTLNLAAN CLDRHLAERG DQTAIIWEGD 100
DPNQSKTVTY KQLHHDVCQF ANVLKSLGVK KGDVVAIYMP MVPEAAVAML 150
ACARIGAVHS VIFGGFSPDA VAGRIIDSHS KLVITADEGI RAGRAIPLKK 200
NVDEALKNPA ITSIKNVVVF QRTGNASYWE DGRDVWWHDL IKEASADCPP 250
EEMNAEDPLF ILYTSGSTGK PKGVVHTTGG YLVYAALTFK YVFDYHPGDI 300
YWCTADVGWV TGHSYLLYGP LACGAITLMF EGVPNYPGVN RLSQVVDKHK 350
VNILYTAPTA IRALMAEGDK AIEGTKRDSL RIMGSVGEPI NPEAWEWYYN 400
KIGNSKCPIV DTWWQTETGG FMITPLPGAT ELKAGSATRP FFGVQPALVD 450
NLGNPQEGVA EGNLVITDSW PGQARTLFGD HERFEQTYFS TFKGMYFSGD 500
GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP KIAEAAVVGV 550
PHNIKGQAIY AYITLNHGEE PTPELYTEVR NWVRKEIGPL ATPDILHWTD 600
SLPKTRSGKI MRRILRKIAT GDTSNLGDTS TLADPSVVEK LLEEKQSMQT 650
PS 652
Length:652
Mass (Da):72,072
Last modified:May 15, 2007 - v1
Checksum:i933CF5A79F7E4D63
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000668 Genomic DNA. Translation: ABP42068.1.
RefSeqiYP_001165041.1. NC_009381.1.

Genome annotation databases

EnsemblBacteriaiABP42068; ABP42068; YPDSF_3718.
GeneIDi5063053.
KEGGiypp:YPDSF_3718.
PATRICi18617513. VBIYerPes122972_4612.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000668 Genomic DNA. Translation: ABP42068.1 .
RefSeqi YP_001165041.1. NC_009381.1.

3D structure databases

ProteinModelPortali A4TS06.
SMRi A4TS06. Positions 5-647.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 386656.YPDSF_3718.

Proteomic databases

PRIDEi A4TS06.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABP42068 ; ABP42068 ; YPDSF_3718 .
GeneIDi 5063053.
KEGGi ypp:YPDSF_3718.
PATRICi 18617513. VBIYerPes122972_4612.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci YPES386656:GKD7-3806-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Pestoides F.

Entry informationi

Entry nameiACSA_YERPP
AccessioniPrimary (citable) accession number: A4TS06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 15, 2007
Last modified: May 14, 2014
This is version 48 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

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