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G7UST0

- G7UST0_PSEUP

UniProt

G7UST0 - G7UST0_PSEUP

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Protein

Acetyl-coenzyme A synthetase

Gene
acsA, DSC_00690
Organism
Pseudoxanthomonas spadix (strain BD-a59)
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 sitei310 – 3101Coenzyme A By similarityUniRule annotation
Binding sitei386 – 3861Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei499 – 4991Substrate By similarityUniRule annotation
Binding sitei514 – 5141Substrate By similarityUniRule annotation
Active sitei516 – 5161 By similarityUniRule annotation
Binding sitei522 – 5221Coenzyme A By similarityUniRule annotation
Binding sitei525 – 5251Substrate By similarityUniRule annotation
Metal bindingi536 – 5361Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi538 – 5381Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi541 – 5411Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei583 – 5831Coenzyme A By similarityUniRule 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 annotation

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotationSAAS annotations, Metal-bindingUniRule annotationSAAS annotations, 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 ligase
Acyl-activating enzyme
Gene namesi
Name:acsAUniRule annotation
Ordered Locus Names:DSC_00690Imported
OrganismiPseudoxanthomonas spadix (strain BD-a59)Imported
Taxonomic identifieri1045855 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaePseudoxanthomonas
ProteomesiUP000005870: Chromosome

PTM / Processingi

Amino acid modifications

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

Structurei

3D structure databases

ProteinModelPortaliG7UST0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni410 – 4156Substrate binding By similarityUniRule annotation

Sequence similaritiesi

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

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MSDLYPVDPA FARQARVDAA TYARDYKASI EQPEAFWKQV AQRLDWIKAP    50
TRIKDVSFDV DDFHIQWFAD GELNASVNCL DRQLEARGDK IALLFEPDSP 100
DSESYGVTYR QLHARVCRLA NALRSLGVAK GDRVTIYLPM IPDAAVAMLA 150
CARIGAVHSV VFGGFAPNSI ADRVADCASK LIITADEGLR GSRKIPLKAN 200
VDAALKLPGT SSVETVLVVR HTGGPVDMQA PRDRWFHDVV DSQPDTCEPE 250
RMNAEDPLFI LYTSGSTGKP KGVLHTTGGY LLWAAYTHEL VFDLKEDDIY 300
WCTADVGWVT GHSYIVYGPL ANGATSLVFE GVPSYPDNSR FWQVVDKHRV 350
SLFYTAPTAI RALMREGDGP VRKTSRKTLR VLGTVGEPIN PEAWRWYYEV 400
VGDSRCPIVD TWWQTETGGH MITPLPGATA LKPGSATVPF FGVQPAVVDA 450
NGVELEGQAE GNLVIKDSWP GQMRTVYGDH QRFIDTYFRT YPGTYFTGDG 500
CRRDADGYYW ITGRVDDVIN VSGHRIGTAE VESALVSHPK VAEAAVVGFP 550
HDLKGQGIYA YVTLVAGEQP TEELRKELIA HVRKEIGPIA SPDHLQWAPG 600
LPKTRSGKIM RRILRKIAEN APDQLGDTST LADPSVVDSL VSERKVR 647
Length:647
Mass (Da):71,329
Last modified:January 25, 2012 - v1
Checksum:i07780B2B3F86F15E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
GeneIDi11374541.
KEGGipsd:DSC_00690.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003093 Genomic DNA. Translation: AER54791.1 .
RefSeqi WP_014162112.1. NC_016147.2.
YP_004928832.1. NC_016147.2.

3D structure databases

ProteinModelPortali G7UST0.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AER54791 ; AER54791 ; DSC_00690 .
GeneIDi 11374541.
KEGGi psd:DSC_00690.

Phylogenomic databases

KOi K01895.

Enzyme and pathway databases

BioCyci PSPA1045855:GH5V-3138-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. "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: September 3, 2014
This is version 15 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

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