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Protein

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

Gene

mshC

Organism
Mycobacterium marinum (strain ATCC BAA-535 / M)
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 sitei226 – 2261Cysteinyl adenylateUniRule annotation
Metal bindingi230 – 2301ZincUniRule annotation
Metal bindingi255 – 2551ZincUniRule annotation
Binding sitei282 – 2821Cysteinyl 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

BioCyciMMAR216594:GJOB-3127-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:MMAR_3110
OrganismiMycobacterium marinum (strain ATCC BAA-535 / M)
Taxonomic identifieri216594 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000001190 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 411411L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligasePRO_0000400462Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi216594.MMAR_3110.

Structurei

3D structure databases

ProteinModelPortaliB2HFY1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni43 – 464Cysteinyl adenylate bindingUniRule annotation
Regioni81 – 833Cysteinyl adenylate bindingUniRule annotation
Regioni248 – 2503Cysteinyl adenylate bindingUniRule annotation

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi45 – 5511"HIGH" regionUniRule annotationAdd
BLAST
Motifi186 – 1916"ERGGDP" regionUniRule annotation
Motifi288 – 2925"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.
OMAiARHYVHT.
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.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERiPTHR10890. PTHR10890. 1 hit.
PfamiPF01406. tRNA-synt_1e. 1 hit.
[Graphical view]
PRINTSiPR00983. TRNASYNTHCYS.
SUPFAMiSSF47323. SSF47323. 1 hit.
TIGRFAMsiTIGR03447. mycothiol_MshC. 1 hit.

Sequencei

Sequence statusi: Complete.

B2HFY1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQSWSSAPVP IVPGRGPELR LYDTADRQVR PVAPGNTATM YVCGITPYDA
60 70 80 90 100
THLGHAATYL AFDLIHRLWL DLGHEVRYVQ NVTDVDDPLF ERADRDGVDW
110 120 130 140 150
RDLAAQEVAL FREDMAALRV LSPHDYVGAT EAVAEIIELV EKLLASGAAY
160 170 180 190 200
VLDGEHPDVY YRSDATLQFG YESGYDRDTM LGLFEQRGGD PGRPGKNDAL
210 220 230 240 250
DALLWRAARP GEPSWPSPFG PGRPGWHIEC AAIALSRVGS GLDVQGGGSD
260 270 280 290 300
LIFPHHEFTA AHAECVTGER RFARHYVHAG MIGWDGHKMS KSRGNLVLVS
310 320 330 340 350
GLRAEGVNPA AVRLGLLAGH YRADRFWSQQ VLDEAVGRLQ RWRAATTLPA
360 370 380 390 400
GPDAAAVVAR VRQYLADDLN TPKAIAALDG WATDALDYGG HDEVAPRLVA
410
STIDALLGVD L
Length:411
Mass (Da):44,728
Last modified:June 10, 2008 - v1
Checksum:i23CBF2D0424DCB32
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000854 Genomic DNA. Translation: ACC41545.1.
RefSeqiWP_012394792.1. NC_010612.1.

Genome annotation databases

EnsemblBacteriaiACC41545; ACC41545; MMAR_3110.
KEGGimmi:MMAR_3110.
PATRICi18067293. VBIMycMar75906_3327.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000854 Genomic DNA. Translation: ACC41545.1.
RefSeqiWP_012394792.1. NC_010612.1.

3D structure databases

ProteinModelPortaliB2HFY1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi216594.MMAR_3110.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACC41545; ACC41545; MMAR_3110.
KEGGimmi:MMAR_3110.
PATRICi18067293. VBIMycMar75906_3327.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciMMAR216594:GJOB-3127-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.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERiPTHR10890. PTHR10890. 1 hit.
PfamiPF01406. tRNA-synt_1e. 1 hit.
[Graphical view]
PRINTSiPR00983. TRNASYNTHCYS.
SUPFAMiSSF47323. SSF47323. 1 hit.
TIGRFAMsiTIGR03447. mycothiol_MshC. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-535 / M.

Entry informationi

Entry nameiMSHC_MYCMM
AccessioniPrimary (citable) accession number: B2HFY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: June 10, 2008
Last modified: January 20, 2016
This is version 46 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.