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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Rhodopseudomonas palustris (strain BisA53)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei308 – 3081Coenzyme AUniRule annotation
Binding sitei332 – 3321Coenzyme AUniRule annotation
Binding sitei497 – 4971ATPUniRule annotation
Binding sitei512 – 5121ATPUniRule annotation
Binding sitei520 – 5201Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei523 – 5231ATPUniRule annotation
Metal bindingi534 – 5341Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi536 – 5361Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi539 – 5391Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei581 – 5811Coenzyme AUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi384 – 3863ATPUniRule annotation
Nucleotide bindingi408 – 4136ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciRPAL316055:GHR9-71-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:acsAUniRule annotation
Ordered Locus Names:RPE_0069
OrganismiRhodopseudomonas palustris (strain BisA53)
Taxonomic identifieri316055 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas
Proteomesi
  • UP000000654 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 648648Acetyl-coenzyme A synthetasePRO_1000065311Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei606 – 6061N6-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

STRINGi316055.RPE_0069.

Structurei

3D structure databases

ProteinModelPortaliQ07VK4.
SMRiQ07VK4. Positions 8-643.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni190 – 1934Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiEGAPNWP.
OrthoDBiPOG091H059D.

Family and domain databases

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.

Q07VK4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEKIYDVPA EWAKRAFVDD AKYQEMYARS VNDPNGFWKD EAQRVDWIKP
60 70 80 90 100
FSVVENTSFA PGNVSIKWFE DGVLNVAANC IDRHLKDRAD QVAIIWEGDD
110 120 130 140 150
PSESRKITYR QLHDEVCKMA NVLRNRNVQK GDRVTIYLPM IPEAAFAMLA
160 170 180 190 200
CARIGAIHSV VFGGFSPDSL AQRITDCASK VVITADEGLR GGRTVPLKAN
210 220 230 240 250
VDAALRKSSA VDWVVVVKRT GADVFMDDVR DFWYHEAAEM VTTECPVEPM
260 270 280 290 300
HAEDPLFILY TSGSTGQPKG VLHTTGGYLV FASMTHQYVF DYHDGDVYWC
310 320 330 340 350
TADVGWVTGH SYILYGPLAN GATTLMFEGV PNYPTNSRFW EVIDKHQVNI
360 370 380 390 400
FYTAPTAIRA LMQGGDEPVT KTSRKSLRLL GSVGEPINPE AWEWYHRVVG
410 420 430 440 450
EDRCPIVDTW WQTETGGILI TPLPGATKLK PGSATRPFFG VVPQIMDADA
460 470 480 490 500
NVLEGECTGN LCLAKSWPGQ MRTVYGDHAR FEQTYFSAYP GKYFTGDGCR
510 520 530 540 550
RDADGYYWIT GRVDDVINVS GHRMGTAEVE SSLVAHPQVS EAAVVGYPHD
560 570 580 590 600
IKGQGIYAYV TLMTGVEPTE ALRKELVAWV RKDIGPIASP DLIQFAPGLP
610 620 630 640
KTRSGKIMRR ILRKIAEDES STLGDTSTLA DPGVVSELVE HRQNKRHV
Length:648
Mass (Da):72,035
Last modified:October 31, 2006 - v1
Checksum:i86B62D4B6EB9B577
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000463 Genomic DNA. Translation: ABJ04030.1.
RefSeqiWP_011661524.1. NC_008435.1.

Genome annotation databases

EnsemblBacteriaiABJ04030; ABJ04030; RPE_0069.
KEGGirpe:RPE_0069.
PATRICi23254602. VBIRhoPal93214_0068.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000463 Genomic DNA. Translation: ABJ04030.1.
RefSeqiWP_011661524.1. NC_008435.1.

3D structure databases

ProteinModelPortaliQ07VK4.
SMRiQ07VK4. Positions 8-643.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi316055.RPE_0069.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABJ04030; ABJ04030; RPE_0069.
KEGGirpe:RPE_0069.
PATRICi23254602. VBIRhoPal93214_0068.

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiEGAPNWP.
OrthoDBiPOG091H059D.

Enzyme and pathway databases

BioCyciRPAL316055:GHR9-71-MONOMER.

Family and domain databases

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_RHOP5
AccessioniPrimary (citable) accession number: Q07VK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 31, 2006
Last modified: September 7, 2016
This is version 60 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

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.