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Protein

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

Gene

mshC

Organism
Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235)
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 bindingi43 – 431ZincUniRule annotation
Binding sitei58 – 581Cysteinyl adenylateUniRule annotation
Binding sitei240 – 2401Cysteinyl adenylateUniRule annotation
Metal bindingi244 – 2441ZincUniRule annotation
Metal bindingi269 – 2691ZincUniRule annotation
Binding sitei295 – 2951Cysteinyl 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

BioCyciRSAL288705:GHX1-2044-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:RSal33209_2044
OrganismiRenibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235)
Taxonomic identifieri288705 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaeRenibacterium
Proteomesi
  • UP000002007 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 423423L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligasePRO_0000400474Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi288705.RSal33209_2044.

Structurei

3D structure databases

ProteinModelPortaliA9WSI9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni43 – 464Cysteinyl adenylate bindingUniRule annotation
Regioni81 – 833Cysteinyl adenylate bindingUniRule annotation
Regioni262 – 2643Cysteinyl adenylate bindingUniRule annotation

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi45 – 5511"HIGH" regionUniRule annotationAdd
BLAST
Motifi199 – 2046"ERGGDP" regionUniRule annotation
Motifi301 – 3055"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.
OMAiILAHHYR.
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.

A9WSI9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSWSTRPLP QLPGNIEAPQ LFDSASKTLR ALPVAADASL YVCGITPYDA
60 70 80 90 100
THMGHAATYL AFDLLGRVWR DSGASVNYVQ NVTDIDDPLL ERADRDGVDW
110 120 130 140 150
RELAESQIEL FRADMTALNV IAPQQYIGAI EAIQWIVPAV EELIAEGFAY
160 170 180 190 200
RMDSGDVYFD TVAASVKTPD SSNAGELGAW WLGQISGLSP EEMLPVFAER
210 220 230 240 250
GGDPERDGKR NPLDPLLWRV ERAGEPAWPG ASLGDGRPGW HIECTVIARK
260 270 280 290 300
FLPAPFSVQG GGSDLLFPHH EMGDGHAWAL DHTPLAKHYA HAGMVGLDGE
310 320 330 340 350
KMSKSRGNLV LVSALRAEGV DPMAVRLSIL ANHYRSDWSW TAELLERSKL
360 370 380 390 400
RLAQWRAAME HTSVGSAAQL VSEIRTALAA DLDAPTALNA VDNWVGQKAT
410 420
TEHSALDAAL ASDAIEALLG VVL
Length:423
Mass (Da):45,829
Last modified:February 5, 2008 - v1
Checksum:iB7ED4F55BA622787
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000910 Genomic DNA. Translation: ABY23777.1.
RefSeqiWP_012245447.1. NC_010168.1.

Genome annotation databases

EnsemblBacteriaiABY23777; ABY23777; RSal33209_2044.
KEGGirsa:RSal33209_2044.
PATRICi23077431. VBIRenSal21953_2132.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000910 Genomic DNA. Translation: ABY23777.1.
RefSeqiWP_012245447.1. NC_010168.1.

3D structure databases

ProteinModelPortaliA9WSI9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi288705.RSal33209_2044.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABY23777; ABY23777; RSal33209_2044.
KEGGirsa:RSal33209_2044.
PATRICi23077431. VBIRenSal21953_2132.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciRSAL288705:GHX1-2044-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. "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests reductive evolution away from an environmental Arthrobacter ancestor."
    Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S., Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H., Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.
    J. Bacteriol. 190:6970-6982(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235.

Entry informationi

Entry nameiMSHC_RENSM
AccessioniPrimary (citable) accession number: A9WSI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: February 5, 2008
Last modified: January 20, 2016
This is version 55 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.