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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Pseudoxanthomonas spadix (strain BD-a59)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei310 – 3101Coenzyme AUniRule annotation
Binding sitei499 – 4991ATPUniRule annotation
Binding sitei514 – 5141ATPUniRule annotation
Binding sitei522 – 5221Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei525 – 5251ATPUniRule annotation
Metal bindingi536 – 5361Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi538 – 5381Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi541 – 5411Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei583 – 5831Coenzyme AUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi386 – 3883ATPUniRule annotation
Nucleotide bindingi410 – 4156ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotation

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciPSPA1045855:GH5V-3138-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:DSC_00690Imported
OrganismiPseudoxanthomonas spadix (strain BD-a59)Imported
Taxonomic identifieri1045855 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaePseudoxanthomonas
ProteomesiUP000005870 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei608 – 6081N6-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

STRINGi1045855.DSC_00690.

Structurei

3D structure databases

ProteinModelPortaliG7UST0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni190 – 1934Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

KOiK01895.

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.

G7UST0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDLYPVDPA FARQARVDAA TYARDYKASI EQPEAFWKQV AQRLDWIKAP
60 70 80 90 100
TRIKDVSFDV DDFHIQWFAD GELNASVNCL DRQLEARGDK IALLFEPDSP
110 120 130 140 150
DSESYGVTYR QLHARVCRLA NALRSLGVAK GDRVTIYLPM IPDAAVAMLA
160 170 180 190 200
CARIGAVHSV VFGGFAPNSI ADRVADCASK LIITADEGLR GSRKIPLKAN
210 220 230 240 250
VDAALKLPGT SSVETVLVVR HTGGPVDMQA PRDRWFHDVV DSQPDTCEPE
260 270 280 290 300
RMNAEDPLFI LYTSGSTGKP KGVLHTTGGY LLWAAYTHEL VFDLKEDDIY
310 320 330 340 350
WCTADVGWVT GHSYIVYGPL ANGATSLVFE GVPSYPDNSR FWQVVDKHRV
360 370 380 390 400
SLFYTAPTAI RALMREGDGP VRKTSRKTLR VLGTVGEPIN PEAWRWYYEV
410 420 430 440 450
VGDSRCPIVD TWWQTETGGH MITPLPGATA LKPGSATVPF FGVQPAVVDA
460 470 480 490 500
NGVELEGQAE GNLVIKDSWP GQMRTVYGDH QRFIDTYFRT YPGTYFTGDG
510 520 530 540 550
CRRDADGYYW ITGRVDDVIN VSGHRIGTAE VESALVSHPK VAEAAVVGFP
560 570 580 590 600
HDLKGQGIYA YVTLVAGEQP TEELRKELIA HVRKEIGPIA SPDHLQWAPG
610 620 630 640
LPKTRSGKIM RRILRKIAEN APDQLGDTST LADPSVVDSL VSERKVR
Length:647
Mass (Da):71,329
Last modified:January 25, 2012 - v1
Checksum:i07780B2B3F86F15E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003093 Genomic DNA. Translation: AER54791.1.
RefSeqiWP_014162112.1. NC_016147.2.
YP_004928832.1. NC_016147.2.

Genome annotation databases

EnsemblBacteriaiAER54791; AER54791; DSC_00690.
KEGGipsd:DSC_00690.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003093 Genomic DNA. Translation: AER54791.1.
RefSeqiWP_014162112.1. NC_016147.2.
YP_004928832.1. NC_016147.2.

3D structure databases

ProteinModelPortaliG7UST0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1045855.DSC_00690.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAER54791; AER54791; DSC_00690.
KEGGipsd:DSC_00690.

Phylogenomic databases

KOiK01895.

Enzyme and pathway databases

BioCyciPSPA1045855:GH5V-3138-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas spadix BD-a59."
    Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.
    J. Bacteriol. 194:544-544(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BD-a59Imported.

Entry informationi

Entry nameiG7UST0_PSEUP
AccessioniPrimary (citable) accession number: G7UST0
Entry historyi
Integrated into UniProtKB/TrEMBL: January 25, 2012
Last sequence update: January 25, 2012
Last modified: June 24, 2015
This is version 23 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

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 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.