SubmitCancel

Skip Header

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

Q01NE9

- Q01NE9_SOLUE

UniProt

Q01NE9 - Q01NE9_SOLUE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Acetyl-coenzyme A synthetase
Gene
acsA, Acid_7927
Organism
Solibacter usitatus (strain Ellin6076)
Status
Unreviewed - 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 By similarity.UniRule annotation

Catalytic activityi

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.UniRule annotation

Cofactori

Magnesium By similarity.UniRule annotationSAAS annotations

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei307 – 3071Coenzyme A By similarityUniRule annotation
Binding sitei383 – 3831Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei496 – 4961Substrate By similarityUniRule annotation
Binding sitei511 – 5111Substrate By similarityUniRule annotation
Active sitei513 – 5131 By similarityUniRule annotation
Binding sitei519 – 5191Coenzyme A By similarityUniRule annotation
Binding sitei522 – 5221Substrate By similarityUniRule annotation
Metal bindingi533 – 5331Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi535 – 5351Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi538 – 5381Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei580 – 5801Coenzyme A By similarityUniRule annotation

GO - Molecular functioni

  1. AMP binding Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. acetate-CoA ligase activity Source: UniProtKB-HAMAP
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. acetyl-CoA biosynthetic process from acetate Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotationImported

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotationSAAS annotations, Metal-bindingUniRule annotationSAAS annotations, Nucleotide-binding

Enzyme and pathway databases

BioCyciSUSI234267:GHSK-7980-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 ligase
Acyl-activating enzyme
Gene namesi
Name:acsAUniRule annotation
Ordered Locus Names:Acid_7927Imported
OrganismiSolibacter usitatus (strain Ellin6076)Imported
Taxonomic identifieri234267 [NCBI]
Taxonomic lineageiBacteriaAcidobacteriaSolibacteresSolibacteralesSolibacteraceaeCandidatus Solibacter
ProteomesiUP000000671: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei605 – 6051N6-acetyllysine By similarityUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi234267.Acid_7927.

Structurei

3D structure databases

ProteinModelPortaliQ01NE9.
SMRiQ01NE9. Positions 10-617.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni407 – 4126Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiAWIWYRD.
OrthoDBiEOG68WR2H.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
InterProiIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. 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

MADANVYPPS AEFVSTANVK GMAGYRALYQ RAAEKPEEFW GELADQELHW    50
FRKWTHVFEW DPPFAKWFAG GKINASYNCI DRHLSTPRKN KVAILWEGEP 100
GDQRMITYQE LHRLVCRFAN VLKARGLKAG DRAIIYMGMV PELPVAVLAC 150
ARLGIIHSVV FGGFSAEALK ARIQDLEAQV VITCDGAWRR GKEVRLKDAV 200
DESLAGCDTV KDVIVYRRTG GSIPMQEGRD HWWHDLDTEA SEVCPAEELD 250
SEHPLYVLYT SGTTGKPKGI VHTTGGYLLQ AHMTMKWVFD LHEEDTYWCT 300
ADIGWVTGHS YIVYGPLSAG ATSVMYEGAP DFPQPDRFWR LIEKYKVNIF 350
YTSPTAIRSF VRQGDQWPNA HDMSSLRLLG SVGEPINPAA WEWYYKVIGK 400
ERCPIVDTWW QTETGAIMIA PMPGAVPLKP GSGTLPLPGV IADIVDLQGN 450
PVEANREGFL IVRRPWPSIA RTLWREPDRY KQAYWERVPG VYLAGDAARR 500
DEDGYFWILG RVDDVMNVSG HRLSTMELES ALVRHPAVAE AAVVGKPHEI 550
TGQAVACFVT LKKGTWDHTA LAEELRKWVA HEIGSFAKPE QIRFTDSLPK 600
TRSGKIMRRL LREIVTSNSV TGDVTTLEDL SVVTRLSAQH DED 643
Length:643
Mass (Da):72,281
Last modified:November 14, 2006 - v1
Checksum:i207212BA2B0D0D0E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000473 Genomic DNA. Translation: ABJ88821.1.
RefSeqiYP_829106.1. NC_008536.1.

Genome annotation databases

EnsemblBacteriaiABJ88821; ABJ88821; Acid_7927.
GeneIDi4424186.
KEGGisus:Acid_7927.
PATRICi32018658. VBICanSol30224_8273.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000473 Genomic DNA. Translation: ABJ88821.1 .
RefSeqi YP_829106.1. NC_008536.1.

3D structure databases

ProteinModelPortali Q01NE9.
SMRi Q01NE9. Positions 10-617.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 234267.Acid_7927.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABJ88821 ; ABJ88821 ; Acid_7927 .
GeneIDi 4424186.
KEGGi sus:Acid_7927.
PATRICi 32018658. VBICanSol30224_8273.

Phylogenomic databases

eggNOGi COG0365.
HOGENOMi HOG000229981.
KOi K01895.
OMAi AWIWYRD.
OrthoDBi EOG68WR2H.

Enzyme and pathway databases

BioCyci SUSI234267:GHSK-7980-MONOMER.

Family and domain databases

HAMAPi MF_01123. Ac_CoA_synth.
InterProi IPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ellin6076.

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: June 11, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

Similar proteinsi