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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
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. 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.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei313Coenzyme AUniRule annotation1
Binding sitei337Coenzyme AUniRule annotation1
Binding sitei503ATPUniRule annotation1
Binding sitei518ATPUniRule annotation1
Binding sitei529ATPUniRule annotation1
Metal bindingi540Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi542Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi545Magnesium; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi389 – 391ATPUniRule annotation3
Nucleotide bindingi413 – 418ATPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

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 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:acsAUniRule annotation
Ordered Locus Names:TTHA1248
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000653291 – 648Acetyl-coenzyme A synthetaseAdd BLAST648

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei612N6-acetyllysineUniRule annotation1

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Interactioni

Protein-protein interaction databases

STRINGi300852.TTHA1248.

Structurei

3D structure databases

ProteinModelPortaliQ5SIW6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni195 – 198Coenzyme A bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiEGAPNWP.
PhylomeDBiQ5SIW6.

Family and domain databases

CDDicd05966. ACS. 1 hit.
HAMAPiMF_01123. Ac_CoA_synth. 1 hit.
InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. 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.

Q5SIW6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRLESVLKE ERVFYPSEEF RKQAHIKSEE EYQRLYEESV RDPEGFWGRV
60 70 80 90 100
ASELHWFEPW RKVLEGDLPH PKWFVGGKTN LSYNALDRHV KTWRRNKAAI
110 120 130 140 150
VWEGEPGEER VLTYHDLWRE VQRFANVLKR LGVKKGDRVT IYLPMIPEAA
160 170 180 190 200
IAMLACTRIG AVHSVVFGGF SAGALADRIK DAEAKVLITA DGGFRRGGIV
210 220 230 240 250
PLKQNADEAL KDATSVEHVV VVRRTGEEVP WTPGRDHWWH ELMEAAPDRC
260 270 280 290 300
DPEPMEAEEP LFILYTSGST GKPKGVLHTT GGYMTYVYYT TKLVFDLKDE
310 320 330 340 350
DVYWCTADVG WITGHSYVVY GPLLNGATTV MYEGAPNWPE PDRFWRIVDK
360 370 380 390 400
YGVTVFYTAP TAIRSFMKWG EGWPGKHRLD SLRLLGTVGE PINPEAWLWY
410 420 430 440 450
YHVIGKGRCP IVDTWWQTET GGIMITTLPG AHAMKPGHAG KPFFGVVPEI
460 470 480 490 500
LDGEHRPVEN PDEGGHLCIT RPWPSMLRTV WGDPERFLQQ YFSQHPGVYF
510 520 530 540 550
SGDGAKRDKD GYYMILGRVD DVLNVAGHRL GTMEIESALV AHPAVAEAAV
560 570 580 590 600
VGRPDPVKGE AIVAFVTLKE GHTPSDALKE ELRAHVAKVI GPIARPDEIR
610 620 630 640
FTDALPKTRS GKIMRRLLRQ IAAGEKEIKG DTSTLEDRSV VERLKEGA
Length:648
Mass (Da):73,086
Last modified:December 21, 2004 - v1
Checksum:i4C9DF47256D2D2BF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71071.1.
RefSeqiWP_011228545.1. NC_006461.1.
YP_144514.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71071; BAD71071; BAD71071.
GeneIDi3168842.
KEGGittj:TTHA1248.
PATRICi23957459. VBITheThe93045_1227.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71071.1.
RefSeqiWP_011228545.1. NC_006461.1.
YP_144514.1. NC_006461.1.

3D structure databases

ProteinModelPortaliQ5SIW6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1248.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71071; BAD71071; BAD71071.
GeneIDi3168842.
KEGGittj:TTHA1248.
PATRICi23957459. VBITheThe93045_1227.

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiEGAPNWP.
PhylomeDBiQ5SIW6.

Family and domain databases

CDDicd05966. ACS. 1 hit.
HAMAPiMF_01123. Ac_CoA_synth. 1 hit.
InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. 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...

Entry informationi

Entry nameiACSA_THET8
AccessioniPrimary (citable) accession number: Q5SIW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 21, 2004
Last modified: November 2, 2016
This is version 76 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.