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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Solibacter usitatus (strain Ellin6076)
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 sitei307Coenzyme AUniRule annotation1
Binding sitei496ATPUniRule annotation1
Binding sitei511ATPUniRule annotation1
Binding sitei519Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei522ATPUniRule annotation1
Metal bindingi533Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi535Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi538Magnesium; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi383 – 385ATPUniRule annotation3
Nucleotide bindingi407 – 412ATPUniRule 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:Acid_7927Imported
OrganismiSolibacter usitatus (strain Ellin6076)Imported
Taxonomic identifieri234267 [NCBI]
Taxonomic lineageiBacteriaAcidobacteriaSolibacteresSolibacteralesSolibacteraceaeCandidatus Solibacter
Proteomesi
  • UP000000671 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei605N6-acetyllysineUniRule annotation1

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi234267.Acid_7927.

Structurei

3D structure databases

ProteinModelPortaliQ01NE9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 79ACAS_NInterPro annotationAdd BLAST55
Domaini88 – 518AMP-bindingInterPro annotationAdd BLAST431
Domaini527 – 605AMP-binding_CInterPro annotationAdd BLAST79

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni189 – 192Coenzyme 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.

Q01NE9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADANVYPPS AEFVSTANVK GMAGYRALYQ RAAEKPEEFW GELADQELHW
60 70 80 90 100
FRKWTHVFEW DPPFAKWFAG GKINASYNCI DRHLSTPRKN KVAILWEGEP
110 120 130 140 150
GDQRMITYQE LHRLVCRFAN VLKARGLKAG DRAIIYMGMV PELPVAVLAC
160 170 180 190 200
ARLGIIHSVV FGGFSAEALK ARIQDLEAQV VITCDGAWRR GKEVRLKDAV
210 220 230 240 250
DESLAGCDTV KDVIVYRRTG GSIPMQEGRD HWWHDLDTEA SEVCPAEELD
260 270 280 290 300
SEHPLYVLYT SGTTGKPKGI VHTTGGYLLQ AHMTMKWVFD LHEEDTYWCT
310 320 330 340 350
ADIGWVTGHS YIVYGPLSAG ATSVMYEGAP DFPQPDRFWR LIEKYKVNIF
360 370 380 390 400
YTSPTAIRSF VRQGDQWPNA HDMSSLRLLG SVGEPINPAA WEWYYKVIGK
410 420 430 440 450
ERCPIVDTWW QTETGAIMIA PMPGAVPLKP GSGTLPLPGV IADIVDLQGN
460 470 480 490 500
PVEANREGFL IVRRPWPSIA RTLWREPDRY KQAYWERVPG VYLAGDAARR
510 520 530 540 550
DEDGYFWILG RVDDVMNVSG HRLSTMELES ALVRHPAVAE AAVVGKPHEI
560 570 580 590 600
TGQAVACFVT LKKGTWDHTA LAEELRKWVA HEIGSFAKPE QIRFTDSLPK
610 620 630 640
TRSGKIMRRL LREIVTSNSV TGDVTTLEDL SVVTRLSAQH DED
Length:643
Mass (Da):72,281
Last modified:November 14, 2006 - v1
Checksum:i207212BA2B0D0D0E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000473 Genomic DNA. Translation: ABJ88821.1.
RefSeqiWP_011689532.1. NC_008536.1.

Genome annotation databases

EnsemblBacteriaiABJ88821; ABJ88821; Acid_7927.
KEGGisus:Acid_7927.
PATRICi32018658. VBICanSol30224_8273.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000473 Genomic DNA. Translation: ABJ88821.1.
RefSeqiWP_011689532.1. NC_008536.1.

3D structure databases

ProteinModelPortaliQ01NE9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi234267.Acid_7927.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABJ88821; ABJ88821; Acid_7927.
KEGGisus:Acid_7927.
PATRICi32018658. VBICanSol30224_8273.

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 nameiQ01NE9_SOLUE
AccessioniPrimary (citable) accession number: Q01NE9
Entry historyi
Integrated into UniProtKB/TrEMBL: November 14, 2006
Last sequence update: November 14, 2006
Last modified: November 2, 2016
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference 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.