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Protein

L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase

Gene

mshC

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi43 – 431ZincBy similarity
Binding sitei58 – 581Cysteinyl adenylateBy similarity
Binding sitei224 – 2241Cysteinyl adenylateBy similarity
Metal bindingi228 – 2281ZincBy similarity
Metal bindingi253 – 2531ZincBy similarity
Binding sitei280 – 2801Cysteinyl adenylate; via amide nitrogen and carbonyl oxygenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase (EC:6.3.1.13)
Short name:
L-Cys:GlcN-Ins ligase
Alternative name(s):
Mycothiol ligase
Short name:
MSH ligase
Gene namesi
Name:mshC
Synonyms:cysS2
Ordered Locus Names:SCO1663
ORF Names:SCI52.05c
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
Proteomesi
  • UP000001973 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 409409L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligasePRO_0000159491Add
BLAST

Proteomic databases

PRIDEiQ9ADA4.

Expressioni

Inductioni

Gradually induced by thiol-oxidant diamide, under (probably indirect) control of SigR.1 Publication

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi100226.SCO1663.

Structurei

3D structure databases

ProteinModelPortaliQ9ADA4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni43 – 464Cysteinyl adenylate bindingBy similarity
Regioni81 – 833Cysteinyl adenylate bindingBy similarity
Regioni246 – 2483Cysteinyl adenylate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi45 – 5511"HIGH" regionAdd
BLAST
Motifi183 – 1886"ERGGDP" region
Motifi286 – 2905"KMSKS" region

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C8N. Bacteria.
COG0215. LUCA.
HOGENOMiHOG000245251.
InParanoidiQ9ADA4.
KOiK15526.
OMAiILAHHYR.
OrthoDBiEOG6RVFXC.
PhylomeDBiQ9ADA4.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_01697. MshC.
InterProiIPR024909. Cys-tRNA/MSH_ligase.
IPR017812. Mycothiol_ligase_MshC.
IPR014729. Rossmann-like_a/b/a_fold.
IPR032678. tRNA-synt_1_cat_dom.
[Graphical view]
PANTHERiPTHR10890. PTHR10890. 1 hit.
PfamiPF01406. tRNA-synt_1e. 1 hit.
[Graphical view]
PRINTSiPR00983. TRNASYNTHCYS.
TIGRFAMsiTIGR03447. mycothiol_MshC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9ADA4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHAWPASEVP ALPGQGRDLR IHDTATGGPV TLDPGPVARI YVCGITPYDA
60 70 80 90 100
THMGHAATYN AFDLVQRVWL DTKRQVHYVQ NVTDVDDPLL ERAVRDGVDW
110 120 130 140 150
TALAEQETAL FREDMTALRM LPPQHYIGAV EAIPGIVPLV ERLRDAGAAY
160 170 180 190 200
ELEGDVYFSV EADPHFGGVS HLDAATMRLL SAERGGDPDR PGKKNPLDPM
210 220 230 240 250
LWMAAREGEP SWDGGTLGRG RPGWHIECVA IALDHLGMGF DVQGGGSDLA
260 270 280 290 300
FPHHEMGASH AQALTGEFPM AKAYVHAGMV GLDGEKMSKS KGNLVFVSQL
310 320 330 340 350
RREGVDPAAI RLTLLAHHYR SDWEWTDQVL QDALARLDRW RAAVSRPDGP
360 370 380 390 400
PAEALVEEIR EALANDLDSP AALAAVDRWA ALQQESGGTD IGAPGVVSRA

VDALLGVAL
Length:409
Mass (Da):44,186
Last modified:June 1, 2001 - v1
Checksum:iF0A2F56AD7C84579
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939109 Genomic DNA. Translation: CAC36366.1.
RefSeqiNP_625938.1. NC_003888.3.
WP_003977162.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAC36366; CAC36366; CAC36366.
GeneIDi1097094.
KEGGisco:SCO1663.
PATRICi23732932. VBIStrCoe124346_1680.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939109 Genomic DNA. Translation: CAC36366.1.
RefSeqiNP_625938.1. NC_003888.3.
WP_003977162.1. NC_003888.3.

3D structure databases

ProteinModelPortaliQ9ADA4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO1663.

Proteomic databases

PRIDEiQ9ADA4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC36366; CAC36366; CAC36366.
GeneIDi1097094.
KEGGisco:SCO1663.
PATRICi23732932. VBIStrCoe124346_1680.

Phylogenomic databases

eggNOGiENOG4105C8N. Bacteria.
COG0215. LUCA.
HOGENOMiHOG000245251.
InParanoidiQ9ADA4.
KOiK15526.
OMAiILAHHYR.
OrthoDBiEOG6RVFXC.
PhylomeDBiQ9ADA4.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_01697. MshC.
InterProiIPR024909. Cys-tRNA/MSH_ligase.
IPR017812. Mycothiol_ligase_MshC.
IPR014729. Rossmann-like_a/b/a_fold.
IPR032678. tRNA-synt_1_cat_dom.
[Graphical view]
PANTHERiPTHR10890. PTHR10890. 1 hit.
PfamiPF01406. tRNA-synt_1e. 1 hit.
[Graphical view]
PRINTSiPR00983. TRNASYNTHCYS.
TIGRFAMsiTIGR03447. mycothiol_MshC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-471 / A3(2) / M145.
  2. "Mycothiol regulates and is regulated by a thiol-specific antisigma factor RsrA and sigma(R) in Streptomyces coelicolor."
    Park J.H., Roe J.H.
    Mol. Microbiol. 68:861-870(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: ATCC BAA-471 / A3(2) / M145.

Entry informationi

Entry nameiMSHC_STRCO
AccessioniPrimary (citable) accession number: Q9ADA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: June 1, 2001
Last modified: January 20, 2016
This is version 86 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.