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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei316 – 3161Coenzyme AUniRule annotation
Binding sitei507 – 5071ATPUniRule annotation
Binding sitei522 – 5221ATPUniRule annotation
Binding sitei530 – 5301Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei533 – 5331ATPUniRule annotation
Metal bindingi544 – 5441Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi546 – 5461Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi549 – 5491Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei591 – 5911Coenzyme AUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi392 – 3943ATPUniRule annotation
Nucleotide bindingi416 – 4216ATPUniRule 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

BioCyciRCAP272942:GJIY-2154-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
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 656656Acetyl-coenzyme A synthetasePRO_0000208384Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei616 – 6161N6-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

STRINGi272942.RCAP_rcc02126.

Structurei

3D structure databases

ProteinModelPortaliO68040.
SMRiO68040. Positions 26-652.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni198 – 2014Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiQRFESIY.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
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.
SMRiO68040. Positions 26-652.
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.
OMAiQRFESIY.

Enzyme and pathway databases

BioCyciRCAP272942:GJIY-2154-MONOMER.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of a 189-kb segment of the chromosome of Rhodobacter capsulatus SB1003."
    Vlcek C., Paces V., Maltsev N., Paces J., Haselkorn R., Fonstein M.
    Proc. Natl. Acad. Sci. U.S.A. 94:9384-9388(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
  2. "Complete genome sequence of the photosynthetic purple nonsulfur bacterium Rhodobacter capsulatus SB 1003."
    Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V., Haselkorn R.
    J. Bacteriol. 192:3545-3546(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-309 / NBRC 16581 / SB1003.

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 11, 2015
This is version 85 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.