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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
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 sitei323Coenzyme AUniRule annotation1
Binding sitei347Coenzyme AUniRule annotation1
Binding sitei512ATPUniRule annotation1
Binding sitei527ATPUniRule annotation1
Binding sitei535Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei538ATPUniRule annotation1
Metal bindingi549Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi551Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi554Magnesium; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi399 – 401ATPUniRule annotation3
Nucleotide bindingi423 – 428ATPUniRule 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:CT1652
OrganismiChlorobium tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
Taxonomic identifieri194439 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum
Proteomesi
  • UP000001007 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002083601 – 659Acetyl-coenzyme A synthetaseAdd BLAST659

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei621N6-acetyllysineUniRule annotation1

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiQ8KBY0.

Interactioni

Protein-protein interaction databases

STRINGi194439.CT1652.

Structurei

3D structure databases

ProteinModelPortaliQ8KBY0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni205 – 208Coenzyme A bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiPMASEDR.
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.

Q8KBY0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATEQTKGQS SESISSVLSE RRKFPPPEAF SSQSHISSME QYEKLYADAA
60 70 80 90 100
ADPDKYWGDL AEQFHWFKKW DSVLEWNAPY AKWFNGGTTN IAYNCLDVHV
110 120 130 140 150
GSWRKNKAAI IWEGEEGNER ILTYGELHRQ VSKFANVLKI AGIKPGDKVA
160 170 180 190 200
IYMGMVPELV IAVLACARVG AVHNVIFAGF AAHAITERVN DSRAKIVICA
210 220 230 240 250
DGTRRRGSTI NLKNIVDEAI INTPSVKNVI VLKVTGEEIH MHDGMDHWWH
260 270 280 290 300
DLMGLAVDEC EPAQVDSEHP LFLLYTSGST GKPKGILHTT AGYMVHAASS
310 320 330 340 350
FKYVFDIKDE DIYFCTADIG WITGHTYIIY GPLLNGATVF MYEGAPNYPQ
360 370 380 390 400
WDRFWDIINR HKITILYTAP TAIRAFIRAG NEWVTKHDLS SLRLLGTVGE
410 420 430 440 450
PINPEAWMWY HKYVGQEKCP IVDTWWQTET GGIMISPMPG ATPTKPGTAT
460 470 480 490 500
RPLPGIMVDV VRKDGTPCNA NEGGYLVVKR PWPSMLRTIY GDNERYEKTY
510 520 530 540 550
WSEFPGMYFT GDGARKDDDG YIWIMGRVDD VVNVSGHRLG TSEVESALVS
560 570 580 590 600
HEAVAEAAVV SRPDEIKGNA LVAFVTLKDG YEGDAKLRDS LGKHVAKEIG
610 620 630 640 650
AIAKPDEIRW AKGLPKTRSG KIMRRLLREL ATSNEIKGDV TTLEDLGVIE

NLREQEDEG
Length:659
Mass (Da):73,576
Last modified:September 26, 2003 - v2
Checksum:i2BB84C9AB13EA034
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006470 Genomic DNA. Translation: AAM72877.1.
RefSeqiNP_662535.2. NC_002932.3.
WP_010933316.1. NC_002932.3.

Genome annotation databases

EnsemblBacteriaiAAM72877; AAM72877; CT1652.
GeneIDi1006138.
KEGGicte:CT1652.
PATRICi21401177. VBIChlTep116050_1493.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006470 Genomic DNA. Translation: AAM72877.1.
RefSeqiNP_662535.2. NC_002932.3.
WP_010933316.1. NC_002932.3.

3D structure databases

ProteinModelPortaliQ8KBY0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi194439.CT1652.

Proteomic databases

PRIDEiQ8KBY0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM72877; AAM72877; CT1652.
GeneIDi1006138.
KEGGicte:CT1652.
PATRICi21401177. VBIChlTep116050_1493.

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiPMASEDR.
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_CHLTE
AccessioniPrimary (citable) accession number: Q8KBY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: September 26, 2003
Last modified: November 2, 2016
This is version 81 of the entry and version 2 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.