Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Ralstonia pickettii (strain 12D)
Status
Unreviewed-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 sitei317Coenzyme AUniRule annotation1
Binding sitei512ATPUniRule annotation1
Binding sitei528ATPUniRule annotation1
Binding sitei536Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei539ATPUniRule annotation1
Metal bindingi550Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi555Magnesium; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi397 – 399ATPUniRule annotation3
Nucleotide bindingi421 – 426ATPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotationImported

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotation, Metal-bindingUniRule annotation, 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:Rpic12D_1775Imported
OrganismiRalstonia pickettii (strain 12D)Imported
Taxonomic identifieri428406 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia
Proteomesi
  • UP000008208 Componenti: Chromosome 1

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei625N6-acetyllysineUniRule annotation1

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliC6BJD4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini32 – 87ACAS_NInterPro annotationAdd BLAST56
Domaini95 – 535AMP-bindingInterPro annotationAdd BLAST441
Domaini544 – 625AMP-binding_CInterPro annotationAdd BLAST82

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni197 – 200Coenzyme A bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000229981.
KOiK01895.
OMAiGPLANGC.
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.

C6BJD4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGIESVLQE TRVFNPPESF VKQANIAGMD AYRALCAEAE KDYEGFWARL
60 70 80 90 100
AHEHLLWHKP FSKVLDESNA PFYKWFEDGE LNASYNCLER NLENGNADKV
110 120 130 140 150
AIIFETDDGN VSRITYRELH ARVCRFANGL KALGIKKGDR VVIYMPMSVE
160 170 180 190 200
GIVAMQACAR IGATHSVVFG GFSAKSLQER IVDVGAVALI TADEQMRGGK
210 220 230 240 250
ALPLKAIADE ALAMEGTGAV KHVIVYRRTN GNVNWVEGRD RAMDEVEAGQ
260 270 280 290 300
PDTCEVTPVS AEHPLFILYT SGSTGKPKGV QHSTGGYLLW ALLTMQWTFD
310 320 330 340 350
LKPDDIFWCT ADIGWVTGHS YIAYGPLAAG ATQVVFEGVP TYPNAGRFWD
360 370 380 390 400
MIQRHKVNTF YTAPTAIRSL IKAAEADEKV HPKQYDLSSL RLLGTVGEPI
410 420 430 440 450
NPEAWMWYHT NIGGGRCPIV DTFWQTETGG HMMTPLPGAT PLVPGSCTLP
460 470 480 490 500
LPGIMAAVVD ETGHDVPNGQ GGILVVKRPW PSMIRTIWGD PERFKKSYFP
510 520 530 540 550
EELGGKLYLA GDGSIRDKET GYFTIMGRID DVLNVSGHRM GTMEIESALV
560 570 580 590 600
ANPIVAEAAV VGRPDDMTGE AICAFVVLKR ARPDGDEAKQ IANELRNWVG
610 620 630 640 650
KEIGPIAKPK DIRFGDNLPK TRSGKIMRRL LRSLAKGEDI TQDTSTLENP
660
AILDQLKETR
Length:660
Mass (Da):72,595
Last modified:September 1, 2009 - v1
Checksum:i5656BD9158B10654
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001644 Genomic DNA. Translation: ACS63057.1.
RefSeqiWP_012762228.1. NC_012856.1.

Genome annotation databases

EnsemblBacteriaiACS63057; ACS63057; Rpic12D_1775.
KEGGirpf:Rpic12D_1775.
PATRICi20242597. VBIRalPic57998_2388.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001644 Genomic DNA. Translation: ACS63057.1.
RefSeqiWP_012762228.1. NC_012856.1.

3D structure databases

ProteinModelPortaliC6BJD4.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACS63057; ACS63057; Rpic12D_1775.
KEGGirpf:Rpic12D_1775.
PATRICi20242597. VBIRalPic57998_2388.

Phylogenomic databases

HOGENOMiHOG000229981.
KOiK01895.
OMAiGPLANGC.
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 nameiC6BJD4_RALP1
AccessioniPrimary (citable) accession number: C6BJD4
Entry historyi
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: November 2, 2016
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

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.