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Q828M2 (MSHC_STRAW) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. 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:SAV_6647
OrganismStreptomyces avermitilis [Complete proteome] [HAMAP]
Taxonomic identifier33903 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length409 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 – 409409L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase HAMAP MF_01697
PRO_0000159489

Regions

Region43 – 464Cysteinyl adenylate binding By similarity
Region81 – 833Cysteinyl adenylate binding By similarity
Region246 – 2483Cysteinyl adenylate binding By similarity
Motif45 – 5511"HIGH" region HAMAP MF_01697
Motif183 – 1886"ERGGDP" region HAMAP MF_01697
Motif286 – 2905"KMSKS" region HAMAP MF_01697

Sites

Metal binding431Zinc By similarity
Metal binding2281Zinc By similarity
Metal binding2531Zinc By similarity
Binding site581Cysteinyl adenylate By similarity
Binding site2241Cysteinyl adenylate By similarity
Binding site2801Cysteinyl adenylate; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q828M2 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 6D63CA8323100F67

FASTA40944,117
        10         20         30         40         50         60 
MHAWPASEVP ALPGEGRDLR IHDTATGGVI PLHPGPVARI YVCGITPYDA THMGHAATYN 

        70         80         90        100        110        120 
AFDLVQRVWL DTKRQVHYVQ NVTDVDDPLL ERAERDGVDW VGLAEKETAL FREDMTALRM 

       130        140        150        160        170        180 
LPPQHYIGAV EAIPGIVPLV ERLRDAGAAY ELDGDVYFSV EADPHFGKVS NLDAAAMRLL 

       190        200        210        220        230        240 
SAERGGDPDR PGKKNPLDPM LWMAAREGEP SWDGASLGRG RPGWHIECVA IALDHLGMGF 

       250        260        270        280        290        300 
DVQGGGSDLA FPHHEMGASH AQALTGEFPM AKAYVHAGMV ALNGEKMSKS KGNLVFVSKL 

       310        320        330        340        350        360 
RRDGVDPAAI RLALLAHHYR SDWEWTDAVL EEALARLGTW RAAVSRPDGP PAEALVEEIR 

       370        380        390        400 
DALANDLDAP AALAAVDRWA ALQHERGGTD EGAPGVVSRA VDALLGVAL

« Hide

References

[1]"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed: 11572948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.
[2]"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
Nat. Biotechnol. 21:526-531(2003) [PubMed: 12692562] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000030 Genomic DNA. Translation: BAC74358.1.
RefSeqNP_827823.1. NC_003155.4.

3D structure databases

ProteinModelPortalQ828M2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1211523.
GenomeReviewsGene locus SAV_6647 in contig BA000030_GR.
KEGGsma:SAV_6647.
NMPDRfig|227882.1.peg.6649.
PATRIC23727398. VBIStrAve112782_7047.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG327651.
OMAALFREDM.
ProtClustDBPRK12418.

Enzyme and pathway databases

BioCycSAVE227882:SAV6647-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_STRAW
AccessionPrimary (citable) accession number: Q828M2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 57 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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