Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

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

Gene

mshC

Organism
Frankia alni (strain ACN14a)
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.UniRule annotation

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.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi15 – 151ZincUniRule annotation
Binding sitei30 – 301Cysteinyl adenylateUniRule annotation
Binding sitei195 – 1951Cysteinyl adenylateUniRule annotation
Metal bindingi199 – 1991ZincUniRule annotation
Metal bindingi224 – 2241ZincUniRule annotation
Binding sitei251 – 2511Cysteinyl adenylate; via amide nitrogen and carbonyl oxygenUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciFALN326424:GJ82-2814-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligaseUniRule annotation (EC:6.3.1.13UniRule annotation)
Short name:
L-Cys:GlcN-Ins ligaseUniRule annotation
Alternative name(s):
Mycothiol ligaseUniRule annotation
Short name:
MSH ligaseUniRule annotation
Gene namesi
Name:mshCUniRule annotation
Ordered Locus Names:FRAAL2858
OrganismiFrankia alni (strain ACN14a)
Taxonomic identifieri326424 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaFrankialesFrankiaceaeFrankia
Proteomesi
  • UP000000657 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 413413L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligasePRO_0000400445Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi326424.FRAAL2858.

Structurei

3D structure databases

ProteinModelPortaliQ0RLV2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni15 – 184Cysteinyl adenylate bindingUniRule annotation
Regioni53 – 553Cysteinyl adenylate bindingUniRule annotation
Regioni217 – 2193Cysteinyl adenylate bindingUniRule annotation

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi17 – 2711"HIGH" regionUniRule annotationAdd
BLAST
Motifi155 – 1606"ERGGDP" regionUniRule annotation
Motifi257 – 2615"KMSKS" regionUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C8N. Bacteria.
COG0215. LUCA.
HOGENOMiHOG000245251.
KOiK15526.
OMAiHANTYVS.
OrthoDBiEOG6RVFXC.

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.

Q0RLV2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRALDSAPTA HLYVCGITPY DATHLGHAFT YLTYDLAQRV LRDSGHKVLY
60 70 80 90 100
VQNVTDVDDP LLERADRDGL DWRDLAAREI ALFREDMTAL RMLAPDSYVG
110 120 130 140 150
VVEAIPMIVD MVAELVDRGA AYHVDDDLYF SVAAAPAFGE ISHLSRAEML
160 170 180 190 200
AICAERGGDP GRGGKKDPLD PLLWRARRPG EPSWPSPFGP GRPGWHIECS
210 220 230 240 250
AIARHHLGGV VDLQGGGTDL SFPHHECSAA HAEVAAGARP FARSYVHTAM
260 270 280 290 300
VSLDGHKMSK SRGNLEFVSR LRRAGTDLAA LRLALLDHRH TADWEWSASL
310 320 330 340 350
LTDAVARVGR WRAAVALPAG PDAQGVLAAV RERLADDLDA PGALAAVDAW
360 370 380 390 400
VDAALADAGG GPVGGSVGVG SSGGSLRGSG GAASAGGEAP ALVARLVDTL
410
LGVDLEPVRP RGS
Length:413
Mass (Da):43,602
Last modified:September 5, 2006 - v1
Checksum:i696C67795BE1CAA3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CT573213 Genomic DNA. Translation: CAJ61502.1.
RefSeqiWP_011604004.1. NC_008278.1.

Genome annotation databases

KEGGifal:FRAAL2858.
PATRICi21915302. VBIFraAln347_2607.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CT573213 Genomic DNA. Translation: CAJ61502.1.
RefSeqiWP_011604004.1. NC_008278.1.

3D structure databases

ProteinModelPortaliQ0RLV2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi326424.FRAAL2858.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGifal:FRAAL2858.
PATRICi21915302. VBIFraAln347_2607.

Phylogenomic databases

eggNOGiENOG4105C8N. Bacteria.
COG0215. LUCA.
HOGENOMiHOG000245251.
KOiK15526.
OMAiHANTYVS.
OrthoDBiEOG6RVFXC.

Enzyme and pathway databases

BioCyciFALN326424:GJ82-2814-MONOMER.

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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ACN14a.

Entry informationi

Entry nameiMSHC_FRAAA
AccessioniPrimary (citable) accession number: Q0RLV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: September 5, 2006
Last modified: January 20, 2016
This is version 66 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.