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P67017 (MSHC_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. 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:Rv2130c, MT2188
ORF Names:MTCY261.29c
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length414 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the ATP-dependent condensation of GlcN-Ins and L-cysteine to form L-Cys-GlcN-Ins. 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. Ref.3

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 caution

The sequence AAK46472.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 414414L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase HAMAP MF_01697
PRO_0000159442

Regions

Region43 – 464Cysteinyl adenylate binding By similarity
Region81 – 833Cysteinyl adenylate binding By similarity
Region251 – 2533Cysteinyl adenylate binding By similarity
Motif45 – 5511"HIGH" region HAMAP MF_01697
Motif189 – 1946"ERGGDP" region HAMAP MF_01697
Motif291 – 2955"KMSKS" region HAMAP MF_01697

Sites

Metal binding431Zinc By similarity
Metal binding2331Zinc By similarity
Metal binding2581Zinc By similarity
Binding site581Cysteinyl adenylate By similarity
Binding site2291Cysteinyl adenylate By similarity
Binding site2851Cysteinyl adenylate; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
P67017 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: B03159DB99B871E7

FASTA41445,595
        10         20         30         40         50         60 
MQSWYCPPVP VLPGRGPQLR LYDSADRQVR PVAPGSKATM YVCGITPYDA THLGHAATYV 

        70         80         90        100        110        120 
TFDLIHRLWL DLGHELHYVQ NITDIDDPLF ERADRDGVDW RDLAQAEVAL FCEDMAALRV 

       130        140        150        160        170        180 
LPPQDYVGAT EAIAEMVELI EKMLACGAAY VIDREMGEYQ DIYFRADATL QFGYESGYDR 

       190        200        210        220        230        240 
DTMLRLCEER GGDPRRPGKS DELDALLWRA ARPGEPSWPS PFGPGRPGWH VECAAIALSR 

       250        260        270        280        290        300 
IGSGLDIQGG GSDLIFPHHE FTAAHAECVS GERRFARHYV HAGMIGWDGH KMSKSRGNLV 

       310        320        330        340        350        360 
LVSALRAQDV EPSAVRLGLL AGHYRADRFW SQQVLDEATA RLHRWRTATA LPAGPAAVDV 

       370        380        390        400        410 
VARVRRYLAD DLDTPKAIAA LDGWVTDAVE YGGHDAGAPK LVATAIDALL GVDL

« Hide

References

« Hide 'large scale' references
[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed: 9634230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"ATP-dependent L-cysteine:1D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase, mycothiol biosynthesis enzyme MshC, is related to class I cysteinyl-tRNA synthetases."
Sareen D., Steffek M., Newton G.L., Fahey R.C.
Biochemistry 41:6885-6890(2002) [PubMed: 12033919] [Abstract]
Cited for: CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842578 Genomic DNA. Translation: CAB10724.1.
AE000516 Genomic DNA. Translation: AAK46472.1. Different initiation.
PIRE70514.
RefSeqNP_216646.1. NC_000962.2.
NP_336658.1. NC_002755.2.

3D structure databases

ProteinModelPortalP67017.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000003463; EBMYCP00000003463; EBMYCG00000003461.
EBMYCT00000072526; EBMYCP00000070585; EBMYCG00000072521.
GeneID887492.
924281.
GenomeReviewsGene locus MT2188 in contig AE000516_GR.
Gene locus Rv2130c in contig AL123456_GR.
KEGGmtc:MT2188.
mtu:Rv2130c.
PATRIC18126570. VBIMycTub22151_2398.
TIGRMT2188.

Organism-specific databases

TubercuListRv2130c.

Phylogenomic databases

GeneTreeEBGT00050000016491.
HOGENOMHBG327651.
OMAALFREDM.
PhylomeDBP67017.
ProtClustDBPRK12418.

Enzyme and pathway databases

ReactomeREACT_27295. Mycobacterium tuberculosis biological processes.

Family and domain databases

HAMAPMF_01697. MshC.
[Tree]
InterProIPR024909. Cys-tRNA/MSH_ligase.
IPR017812. Mycothiol_ligase_MshC.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[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.
SUPFAMSSF47323. tRNAsyn_1a_bind. 1 hit.
TIGRFAMsTIGR03447. Mycothiol_MshC. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMSHC_MYCTU
AccessionPrimary (citable) accession number: P67017
Secondary accession number(s): O33264
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: January 25, 2012
This is version 52 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents