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Q8NQC4 (MSHC_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase
Short name=L-Cys:GlcN-Ins ligase
EC=6.3.1.13
Alternative name(s):
Mycothiol ligase
Short name=MSH ligase
Gene names
Name:mshC
Synonyms:cysS2
Ordered Locus Names:Cgl1514, cg1709
OrganismCorynebacterium glutamicum (Brevibacterium flavum)
Taxonomic identifier1718 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length404 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the ATP-dependent condensation of GlcN-Ins and L-cysteine to form L-Cys-GlcN-Ins By similarity. HAMAP MF_01697

Catalytic activity

1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + L-cysteine + ATP = 1-O-(2-(L-cysteinamido)-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + AMP + diphosphate. HAMAP MF_01697

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_01697

Subunit structure

Monomer By similarity. HAMAP MF_01697

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. MshC subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 404404L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase HAMAP MF_01697
PRO_0000159389

Regions

Region32 – 354Cysteinyl adenylate binding By similarity
Region70 – 723Cysteinyl adenylate binding By similarity
Region238 – 2403Cysteinyl adenylate binding By similarity
Motif34 – 4411"HIGH" region HAMAP MF_01697
Motif176 – 1816"ERGGDP" region HAMAP MF_01697
Motif278 – 2825"KMSKS" region HAMAP MF_01697

Sites

Metal binding321Zinc By similarity
Metal binding2201Zinc By similarity
Metal binding2451Zinc By similarity
Binding site471Cysteinyl adenylate By similarity
Binding site2161Cysteinyl adenylate By similarity
Binding site2721Cysteinyl adenylate; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8NQC4 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: DCC40EA5B0C06956

FASTA40444,115
        10         20         30         40         50         60 
MPLELFDTAD QEVRLVETPP AGSDTPVGMY VCGITPYDST HLGHAATYLA FDLIYRILLD 

        70         80         90        100        110        120 
NDHDVHYVQN ITDVDDPLFE RAARDGVDWR DLGTSQINLF RSDMEALSII PPKDYIGAIE 

       130        140        150        160        170        180 
SIDEVIEMVK TLLDEGAAYI VEDAEYPDVY ASINATDKFG YESNYDAATM AEFFAERGGD 

       190        200        210        220        230        240 
PERPGKKNPM DALLWRAARE GEPSWESPFG AGRPGWHIEC SAIATNRLGH SFDIQGGGSD 

       250        260        270        280        290        300 
LIFPHHEFSA AHAEAAHGVE RMAKHYVHAG MISQDGVKMS KSLGNLEFVS RLTAAGHEPG 

       310        320        330        340        350        360 
AIRLGVFANH YRGNRDWNAE SLATAEQRLA TWREAARAAT NREDAIAVVE QLRAHLSADL 

       370        380        390        400 
DTPGALAAVD NWAAGIDTTT DSKEFTEVGN IVVAAIDALL GVQL

« Hide

References

[1]"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."
Nakagawa S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000036 Genomic DNA. Translation: BAB98907.1.
BX927152 Genomic DNA. Translation: CAF21523.1.
RefSeqNP_600730.1. NC_003450.3.
YP_225799.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ8NQC4.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1019487.
3345551.
GenomeReviewsGene locus Cgl1514 in contig BA000036_GR.
Gene locus cg1709 in contig BX927147_GR.
KEGGcgb:cg1709.
cgl:NCgl1457.
PATRIC21495073. VBICorGlu203724_1482.

Phylogenomic databases

HOGENOMHBG327651.
OMAALFREDM.
ProtClustDBPRK12418.

Enzyme and pathway databases

BioCycCGLU196627:CG1709-MONOMER.

Family and domain databases

HAMAPMF_01697. MshC.
[Tree]
InterProIPR024909. Cys-tRNA/MSH_ligase.
IPR017812. Mycothiol_ligase_MshC.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
KOK15526.
PANTHERPTHR10890. Cys_tRNA-synt_1a. 1 hit.
PfamPF01406. tRNA-synt_1e. 1 hit.
[Graphical view]
PRINTSPR00983. TRNASYNTHCYS.
TIGRFAMsTIGR03447. Mycothiol_MshC. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMSHC_CORGL
AccessionPrimary (citable) accession number: Q8NQC4
Secondary accession number(s): Q6M572
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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