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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
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 sitei316Coenzyme AUniRule annotation1
Binding sitei507ATPUniRule annotation1
Binding sitei522ATPUniRule annotation1
Binding sitei530Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei533ATPUniRule annotation1
Metal bindingi544Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi546Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi549Magnesium; via carbonyl oxygenUniRule annotation1
Binding sitei591Coenzyme AUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi392 – 394ATPUniRule annotation3
Nucleotide bindingi416 – 421ATPUniRule 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
Synonyms:acs
Ordered Locus Names:RCAP_rcc02126
OrganismiRhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Taxonomic identifieri272942 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
Proteomesi
  • UP000002361 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002083841 – 656Acetyl-coenzyme A synthetaseAdd BLAST656

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei616N6-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

STRINGi272942.RCAP_rcc02126.

Structurei

3D structure databases

ProteinModelPortaliO68040.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni198 – 201Coenzyme A bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

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

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.

O68040-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVQGQPSVA PALREVPAGF ETAHANGAKY LEMYRESLEN PDAFWGREGK
60 70 80 90 100
RLDWITPYTK VKNTDFTFGK VSIKWFEDGV LNASVNCIDR HLRDRALQTA
110 120 130 140 150
IIFEPDDPKE PARHITYKEL SEKVNRMANV LLSQGIMRGD RVVIYLPMIP
160 170 180 190 200
EAAYAMLACA RIGAIHSIVF AGFSPDALAN RINDCGAKLV ITADTAPRGG
210 220 230 240 250
RRTPLKANTD AALLHCSDKV RCLVVKHTGD QISWVHGRDV DLLYLMEHVS
260 270 280 290 300
PECPPRPMNA EDPLFILYTS GSTGKPKGVV HTTGGYLVYA AMTHQYTFDY
310 320 330 340 350
KDGDVFWCTA DVGWVTGHSY IIYGPLANGA TTLMFEGVPT FPDAGRFWAV
360 370 380 390 400
CEKHKVNQFY TAPTAIRALM GQGPEWVEKY DLSSLRVLGS VGEPINPEAW
410 420 430 440 450
VWYDKYVGKG KCPIVDTFWQ TETGGHMITP LPGATPTKPG SATNPFFGVK
460 470 480 490 500
PVVLDPQTAV RIGEVECEGV LCISDSWPGQ MRTVWGDHDR FQETYFGQYR
510 520 530 540 550
GYYFTGDGCR RDKDGYYWIT GRVDDVINVS GHRMGTAEVE SALVAHPQVA
560 570 580 590 600
EAAVVGYPHD IKGQGIYAYV TLMNGIEPSE DLRKDLVKWV RTEIGPIASP
610 620 630 640 650
DLIQWAPGLP KTRSGKIMRR ILRKIAENDY GALGDISTLA DPGVVQELID

NRMNRA
Length:656
Mass (Da):72,703
Last modified:August 1, 1998 - v1
Checksum:i706EA969331D71C2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF010496 Genomic DNA. Translation: AAC16126.1.
CP001312 Genomic DNA. Translation: ADE85856.1.
PIRiT03473.
RefSeqiWP_013067835.1. NC_014034.1.

Genome annotation databases

EnsemblBacteriaiADE85856; ADE85856; RCAP_rcc02126.
KEGGircp:RCAP_rcc02126.
PATRICi35504422. VBIRhoCap134200_2162.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF010496 Genomic DNA. Translation: AAC16126.1.
CP001312 Genomic DNA. Translation: ADE85856.1.
PIRiT03473.
RefSeqiWP_013067835.1. NC_014034.1.

3D structure databases

ProteinModelPortaliO68040.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272942.RCAP_rcc02126.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADE85856; ADE85856; RCAP_rcc02126.
KEGGircp:RCAP_rcc02126.
PATRICi35504422. VBIRhoCap134200_2162.

Phylogenomic databases

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

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_RHOCB
AccessioniPrimary (citable) accession number: O68040
Secondary accession number(s): D5AV74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: November 2, 2016
This is version 88 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.