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Q01NE9

- Q01NE9_SOLUE

UniProt

Q01NE9 - Q01NE9_SOLUE

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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

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.UniRule annotation

Catalytic activityi

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

Cofactori

Magnesium.UniRule annotationSAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei307 – 3071Coenzyme AUniRule annotation
Binding sitei496 – 4961ATPUniRule annotation
Binding sitei511 – 5111ATPUniRule annotation
Binding sitei519 – 5191Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei522 – 5221ATPUniRule annotation
Metal bindingi533 – 5331Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi535 – 5351Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi538 – 5381Magnesium; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi383 – 3853ATPUniRule annotation
Nucleotide bindingi407 – 4126ATPUniRule annotation

GO - Molecular functioni

  1. acetate-CoA ligase activity Source: UniProtKB-HAMAP
  2. AMP binding Source: InterPro
  3. ATP binding Source: UniProtKB-KW
  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 annotation, Metal-bindingUniRule annotationSAAS annotation, 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 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
ProteomesiUP000000671: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei605 – 6051N6-acetyllysineUniRule annotation

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.
SMRiQ01NE9. Positions 10-617.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni189 – 1924Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

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

        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:
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: Ellin6076Imported.

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: October 29, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3