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Protein

Mycothiol acetyltransferase

Gene

mshD

Organism
Corynebacterium glutamicum (strain R)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.UniRule annotation

Catalytic activityi

Desacetylmycothiol + acetyl-CoA = CoA + mycothiol.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei40Desacetylmycothiol; via amide nitrogenUniRule annotation1
Binding sitei179DesacetylmycothiolUniRule annotation1
Binding sitei218DesacetylmycothiolUniRule annotation1
Binding sitei226DesacetylmycothiolUniRule annotation1
Binding sitei264Desacetylmycothiol; via carbonyl oxygenUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Mycothiol acetyltransferaseUniRule annotation (EC:2.3.1.189UniRule annotation)
Short name:
MSH acetyltransferaseUniRule annotation
Alternative name(s):
Mycothiol synthaseUniRule annotation
Gene namesi
Name:mshDUniRule annotation
Ordered Locus Names:cgR_2479
OrganismiCorynebacterium glutamicum (strain R)
Taxonomic identifieri340322 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000006698 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004002511 – 292Mycothiol acetyltransferaseAdd BLAST292

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA4QGX4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini13 – 168N-acetyltransferase 1UniRule annotationAdd BLAST156
Domaini159 – 292N-acetyltransferase 2UniRule annotationAdd BLAST134

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni77 – 79Acetyl-CoA binding 1UniRule annotation3
Regioni230 – 232Acetyl-CoA binding 2UniRule annotation3
Regioni237 – 243Acetyl-CoA binding 2UniRule annotation7

Sequence similaritiesi

Belongs to the acetyltransferase family. MshD subfamily.UniRule annotation
Contains 2 N-acetyltransferase domains.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000248937.
KOiK15520.
OMAiMLYVDES.
OrthoDBiPOG091H09IL.

Family and domain databases

Gene3Di3.40.630.30. 2 hits.
HAMAPiMF_01698. MshD. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
IPR017813. Mycothiol_AcTrfase.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
PF13508. Acetyltransf_7. 1 hit.
[Graphical view]
PIRSFiPIRSF021524. MSH_acetyltransferase. 1 hit.
SUPFAMiSSF55729. SSF55729. 2 hits.
TIGRFAMsiTIGR03448. mycothiol_MshD. 1 hit.
PROSITEiPS51186. GNAT. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A4QGX4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTSDRIKST QIALDRDLRE QALLLLKEVR AVDGVDAFSE QFVRGLAEPG
60 70 80 90 100
LGHSHLIVTL NDKLVGLAAT DEETTELAVH PAHRRQGIGK ALIDAAPTSS
110 120 130 140 150
IWAHGNTAGA QALASTLRMK KTRELLVMEI SDRALDGSAA YKDPDGITHS
160 170 180 190 200
SLANAPVEKS VAEAKWLQSN NEAFDWHPEQ GGWTTHRLAQ AQKADWYKDS
210 220 230 240 250
DVLFLWDGEE IVGFHWVKQH SPELQEIYVV GLSSAYRGRG LGDPLVRLGL
260 270 280 290
HHMRAHGARK VILYVEADNT PAVAAYEKLG FTVAESHVVY EK
Length:292
Mass (Da):32,138
Last modified:May 15, 2007 - v1
Checksum:i8819573D25E88F8B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009044 Genomic DNA. Translation: BAF55490.1.
RefSeqiWP_011897834.1. NC_009342.1.

Genome annotation databases

EnsemblBacteriaiBAF55490; BAF55490; cgR_2479.
KEGGicgt:cgR_2479.
PATRICi21509638. VBICorGlu58097_2542.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009044 Genomic DNA. Translation: BAF55490.1.
RefSeqiWP_011897834.1. NC_009342.1.

3D structure databases

ProteinModelPortaliA4QGX4.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAF55490; BAF55490; cgR_2479.
KEGGicgt:cgR_2479.
PATRICi21509638. VBICorGlu58097_2542.

Phylogenomic databases

HOGENOMiHOG000248937.
KOiK15520.
OMAiMLYVDES.
OrthoDBiPOG091H09IL.

Family and domain databases

Gene3Di3.40.630.30. 2 hits.
HAMAPiMF_01698. MshD. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
IPR017813. Mycothiol_AcTrfase.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
PF13508. Acetyltransf_7. 1 hit.
[Graphical view]
PIRSFiPIRSF021524. MSH_acetyltransferase. 1 hit.
SUPFAMiSSF55729. SSF55729. 2 hits.
TIGRFAMsiTIGR03448. mycothiol_MshD. 1 hit.
PROSITEiPS51186. GNAT. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMSHD_CORGB
AccessioniPrimary (citable) accession number: A4QGX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: May 15, 2007
Last modified: November 2, 2016
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.