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Protein

1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase

Gene

mshB

Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the deacetylation of 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside (GlcNAc-Ins) in the mycothiol biosynthesis pathway.UniRule annotation

Catalytic activityi

1-O-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + H2O = 1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + acetate.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi29 – 291ZincUniRule annotation
Metal bindingi32 – 321ZincUniRule annotation
Metal bindingi162 – 1621ZincUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciCEFF196164:GJW8-1177-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylaseUniRule annotation (EC:3.5.1.103UniRule annotation)
Short name:
GlcNAc-Ins deacetylaseUniRule annotation
Alternative name(s):
N-acetyl-1-D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase
Gene namesi
Name:mshBUniRule annotation
Ordered Locus Names:CE1158
OrganismiCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Taxonomic identifieri196164 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000001409 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3113111D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylasePRO_0000400177Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi196164.HMPREF0290_1304.

Structurei

3D structure databases

ProteinModelPortaliQ8FQG1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the MshB deacetylase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108KZ5. Bacteria.
COG2120. LUCA.
HOGENOMiHOG000241173.
KOiK15525.
OMAiHATQLWV.
OrthoDBiEOG6NSGK1.

Family and domain databases

Gene3Di3.40.50.10320. 1 hit.
HAMAPiMF_01696. MshB.
InterProiIPR003737. GlcNAc_PI_deacetylase-related.
IPR024078. LmbE-like_dom.
IPR017810. Mycothiol_biosynthesis_MshB.
[Graphical view]
PANTHERiPTHR12993. PTHR12993. 1 hit.
PfamiPF02585. PIG-L. 1 hit.
[Graphical view]
SUPFAMiSSF102588. SSF102588. 1 hit.
TIGRFAMsiTIGR03445. mycothiol_MshB. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8FQG1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASRAQRTGG RMILHNDLSG LRVVAVHAHP DDEAITTGGA LHHLATRGAD
60 70 80 90 100
VTVVTCTLGE QGEVIGETWQ QLVNGDADQL GGFRIHELLS SLRILGASGC
110 120 130 140 150
FLGGAGRWRD SGMVGDPAND HPRSFVRSGD QAEEQLVEIF TMLRPHLVIT
160 170 180 190 200
YGPDGGYGHP DHIRAHEITH GAAGRVEGIQ RILWAVTGRT DLQAGLDAIS
210 220 230 240 250
AVPTGWRAAG DDELACQDRV DFALELDDRA YHAKVESMRA HATQLWIADG
260 270 280 290 300
GVSDTNPHAA FAEVTDRAAA PVVFALSNLI AQPVMRREHY QLGAGTAFPA
310
DAQGPADGLQ W
Length:311
Mass (Da):33,230
Last modified:March 1, 2003 - v1
Checksum:i83D98137727D7E8E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000035 Genomic DNA. Translation: BAC17968.1.

Genome annotation databases

EnsemblBacteriaiBAC17968; BAC17968; BAC17968.
KEGGicef:CE1158.
PATRICi21488448. VBICorEff9312_1158.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000035 Genomic DNA. Translation: BAC17968.1.

3D structure databases

ProteinModelPortaliQ8FQG1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196164.HMPREF0290_1304.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC17968; BAC17968; BAC17968.
KEGGicef:CE1158.
PATRICi21488448. VBICorEff9312_1158.

Phylogenomic databases

eggNOGiENOG4108KZ5. Bacteria.
COG2120. LUCA.
HOGENOMiHOG000241173.
KOiK15525.
OMAiHATQLWV.
OrthoDBiEOG6NSGK1.

Enzyme and pathway databases

BioCyciCEFF196164:GJW8-1177-MONOMER.

Family and domain databases

Gene3Di3.40.50.10320. 1 hit.
HAMAPiMF_01696. MshB.
InterProiIPR003737. GlcNAc_PI_deacetylase-related.
IPR024078. LmbE-like_dom.
IPR017810. Mycothiol_biosynthesis_MshB.
[Graphical view]
PANTHERiPTHR12993. PTHR12993. 1 hit.
PfamiPF02585. PIG-L. 1 hit.
[Graphical view]
SUPFAMiSSF102588. SSF102588. 1 hit.
TIGRFAMsiTIGR03445. mycothiol_MshB. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
    Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
    Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Entry informationi

Entry nameiMSHB_COREF
AccessioniPrimary (citable) accession number: Q8FQG1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: March 1, 2003
Last modified: December 9, 2015
This is version 69 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, Reference 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.