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Protein

Acetyl-coenzyme A synthetase

Gene

acs

Organism
Yersinia pseudotuberculosis serotype I (strain IP32953)
Status
Reviewed-Annotation score: 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.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.UniRule annotation

Catalytic activityi

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.UniRule annotation

Cofactori

Mg2+UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei311 – 3111Coenzyme AUniRule annotation
Binding sitei335 – 3351Coenzyme AUniRule annotation
Binding sitei500 – 5001ATPUniRule annotation
Binding sitei515 – 5151ATPUniRule annotation
Binding sitei523 – 5231Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei526 – 5261ATPUniRule annotation
Metal bindingi537 – 5371Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi539 – 5391Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi542 – 5421Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei584 – 5841Coenzyme AUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi387 – 3893ATPUniRule annotation
Nucleotide bindingi411 – 4166ATPUniRule 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

Ligase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciYPSE273123:GI1M-338-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 ligaseUniRule annotation
Acyl-activating enzymeUniRule annotation
Gene namesi
Name:acsUniRule annotation
Ordered Locus Names:YPTB0308
OrganismiYersinia pseudotuberculosis serotype I (strain IP32953)
Taxonomic identifieri273123 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000001011: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 652652Acetyl-coenzyme A synthetasePRO_1000065337Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei609 – 6091N6-acetyllysineUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Interactioni

Protein-protein interaction databases

STRINGi273123.YPTB0308.

Structurei

3D structure databases

ProteinModelPortaliQ66FM8.
SMRiQ66FM8. Positions 5-647.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni191 – 1944Coenzyme A bindingUniRule annotation

Sequence similaritiesi

Belongs to the ATP-dependent AMP-binding enzyme family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiKGKPYML.
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.

Q66FM8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQIHKHPIP AAIAEHALIT PEKYQHYYQQ SVQNPDEFWG EQGKIIDWIK
60 70 80 90 100
PYKTVKNTSF DPGHVSIRWF EDGTLNLAAN CLDRHLAERG DQTAIIWEGD
110 120 130 140 150
DPNQSKTVTY KQLHHDVCQF ANVLKSLGIK KGDVVAIYMP MVPEAAVAML
160 170 180 190 200
ACARIGAVHS VIFGGFSPDA VAGRIIDSHS KLVITADEGI RAGRAIPLKK
210 220 230 240 250
NVDEALKNPA ITSIKNVVVF QRTGNASYWE DGRDVWWHDL IKEASADCPP
260 270 280 290 300
EEMNAEDPLF ILYTSGSTGK PKGVVHTTGG YLVYAALTFK YVFDYHPGDI
310 320 330 340 350
YWCTADVGWV TGHSYLLYGP LACGAITLMF EGVPNYPGVN RLSQVVDKHK
360 370 380 390 400
VNILYTAPTA IRALMAEGDK AIEGTKRDSL RIMGSVGEPI NPEAWEWYYN
410 420 430 440 450
KIGNSKCPIV DTWWQTETGG FMITPLPGAT ELKAGSATRP FFGVQPALVD
460 470 480 490 500
NLGNPQEGVA EGNLVITDSW PGQARTLFGD HDRFEQTYFS TFKGMYFSGD
510 520 530 540 550
GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP KIAEAAVVGV
560 570 580 590 600
PHNIKGQAIY AYITLNHGEE PTPELYTEVR NWVRKEIGPL ATPDILHWTD
610 620 630 640 650
SLPKTRSGKI MRRILRKIAT GDTSNLGDTS TLADPSVVEK LLEEKQSMQT

PS
Length:652
Mass (Da):72,072
Last modified:October 11, 2004 - v1
Checksum:i92FA2E582F1F7B76
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX936398 Genomic DNA. Translation: CAH19548.1.
RefSeqiYP_068854.1. NC_006155.1.

Genome annotation databases

EnsemblBacteriaiCAH19548; CAH19548; YPTB0308.
GeneIDi2956405.
KEGGiyps:YPTB0308.
PATRICi18638765. VBIYerPse22266_0482.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX936398 Genomic DNA. Translation: CAH19548.1.
RefSeqiYP_068854.1. NC_006155.1.

3D structure databases

ProteinModelPortaliQ66FM8.
SMRiQ66FM8. Positions 5-647.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273123.YPTB0308.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAH19548; CAH19548; YPTB0308.
GeneIDi2956405.
KEGGiyps:YPTB0308.
PATRICi18638765. VBIYerPse22266_0482.

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiKGKPYML.
OrthoDBiEOG68WR2H.

Enzyme and pathway databases

BioCyciYPSE273123:GI1M-338-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: IP32953.

Entry informationi

Entry nameiACSA_YERPS
AccessioniPrimary (citable) accession number: Q66FM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 11, 2004
Last modified: January 7, 2015
This is version 63 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.