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Protein

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

Gene

mshC

Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 bindingi48 – 481ZincBy similarity
Binding sitei63 – 631Cysteinyl adenylateBy similarity
Binding sitei232 – 2321Cysteinyl adenylateBy similarity
Metal bindingi236 – 2361ZincBy similarity
Metal bindingi261 – 2611ZincBy similarity
Binding sitei288 – 2881Cysteinyl 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:CE1639
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 – 430430L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligasePRO_0000159387Add
BLAST

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi196164.HMPREF0290_1673.

Structurei

3D structure databases

ProteinModelPortaliQ8FTD0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 514Cysteinyl adenylate bindingBy similarity
Regioni86 – 883Cysteinyl adenylate bindingBy similarity
Regioni254 – 2563Cysteinyl adenylate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi50 – 6011"HIGH" regionAdd
BLAST
Motifi192 – 1976"ERGGDP" region
Motifi294 – 2985"KMSKS" region

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C8N. Bacteria.
COG0215. LUCA.
HOGENOMiHOG000245251.
KOiK15526.
OMAiILAHHYR.
OrthoDBiPOG091H004K.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_01697. MshC. 1 hit.
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.

Q8FTD0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHSWPTPDIP ALDGTPVPLA LYDTADQQVK PVEVPPSGSG TPVGMYVCGI
60 70 80 90 100
TPYDSTHLGH AATYLAFDLI YRVLLDNDHQ VHYVQNITDV DDPLFERAER
110 120 130 140 150
DGVDWRELGT SQIDLFRKDM ETLAVIPPKD YIGAIESIDE VIEMVSTLLE
160 170 180 190 200
EGAAYVVDDP EYPDVYASIN ATENFGYESN YDAATMAELF AERGGDPDRP
210 220 230 240 250
GKRNPMDALL WRAAREGEPS WESPFGPGRP GWHIECSAIA TNRLGHSFDI
260 270 280 290 300
QGGGSDLMFP HHEFSAAHAE AAHGVERMAK HYVHAGMISQ DGVKMSKSLG
310 320 330 340 350
NLEFVHRLTA AGHEPGAIRL GVYAHHYRGD RDWSDEILAA AEARLALWRS
360 370 380 390 400
AITVATDVQA AVDAVAQLRT HLSNDLDTPA ALAAVDAWAE AALKDTGNVS
410 420 430
DTADQFDTPE FTPAGRILAA AVDALLGVRL
Length:430
Mass (Da):46,764
Last modified:March 1, 2003 - v1
Checksum:i1494EABC26B507D2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000035 Genomic DNA. Translation: BAC18449.1.
RefSeqiWP_006767639.1. NZ_GG700683.1.

Genome annotation databases

EnsemblBacteriaiBAC18449; BAC18449; BAC18449.
KEGGicef:CE1639.
PATRICi21489419. VBICorEff9312_1632.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000035 Genomic DNA. Translation: BAC18449.1.
RefSeqiWP_006767639.1. NZ_GG700683.1.

3D structure databases

ProteinModelPortaliQ8FTD0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196164.HMPREF0290_1673.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC18449; BAC18449; BAC18449.
KEGGicef:CE1639.
PATRICi21489419. VBICorEff9312_1632.

Phylogenomic databases

eggNOGiENOG4105C8N. Bacteria.
COG0215. LUCA.
HOGENOMiHOG000245251.
KOiK15526.
OMAiILAHHYR.
OrthoDBiPOG091H004K.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_01697. MshC. 1 hit.
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...

Entry informationi

Entry nameiMSHC_COREF
AccessioniPrimary (citable) accession number: Q8FTD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 1, 2003
Last modified: September 7, 2016
This is version 83 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.