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Protein

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

Gene

mshC

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

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.1 Publication

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Kineticsi

  1. KM=40 µM for L-cysteine2 Publications
  2. KM=72 µM for GlcN-Ins2 Publications
  3. KM=1.84 mM for ATP2 Publications
  1. Vmax=83 nmol/min/mg enzyme2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi43Zinc1 Publication1
Binding sitei58Cysteinyl adenylate1
Binding sitei227Cysteinyl adenylate1
Metal bindingi231Zinc1 Publication1
Metal bindingi256Zinc1 Publication1
Binding sitei283Cysteinyl adenylate; via amide nitrogen and carbonyl oxygen1

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

BioCyciMetaCyc:MONOMER-9641.
MetaCyc:MONOMER-9682.

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:MSMEG_4189, MSMEI_4091
OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Taxonomic identifieri246196 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000006158 Componenti: Chromosome
  • UP000000757 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi46T → V: 100-fold decrease in catalytic turnover. 1 Publication1
Mutagenesisi55H → A: 40-fold decrease in catalytic turnover. 1 Publication1
Mutagenesisi83T → V: Almost no effect. 1 Publication1
Mutagenesisi227W → F or H: 100-fold decrease in catalytic turnover. 1 Publication1
Mutagenesisi251D → A: 1200-fold decfrease in catalytic turnover. 1 Publication1
Mutagenesisi251D → N: 400-fold decrease in catalytic turnover. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003998271 – 412L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligaseAdd BLAST412

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

STRINGi246196.MSMEG_4189.

Structurei

Secondary structure

1412
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi20 – 23Combined sources4
Turni24 – 27Combined sources4
Beta strandi28 – 31Combined sources4
Beta strandi36 – 42Combined sources7
Helixi53 – 71Combined sources19
Beta strandi75 – 82Combined sources8
Helixi87 – 96Combined sources10
Helixi100 – 117Combined sources18
Beta strandi124 – 128Combined sources5
Helixi129 – 131Combined sources3
Helixi133 – 145Combined sources13
Beta strandi148 – 151Combined sources4
Beta strandi160 – 162Combined sources3
Turni168 – 174Combined sources7
Helixi178 – 187Combined sources10
Beta strandi203 – 208Combined sources6
Beta strandi222 – 225Combined sources4
Helixi227 – 238Combined sources12
Beta strandi243 – 249Combined sources7
Helixi250 – 252Combined sources3
Turni253 – 255Combined sources3
Helixi256 – 268Combined sources13
Beta strandi273 – 280Combined sources8
Helixi300 – 305Combined sources6
Helixi310 – 318Combined sources9
Helixi330 – 347Combined sources18
Helixi356 – 367Combined sources12
Helixi372 – 389Combined sources18
Beta strandi392 – 395Combined sources4
Helixi396 – 408Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3C8ZX-ray1.60A/B1-412[»]
ProteinModelPortaliA0QZY0.
SMRiA0QZY0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA0QZY0.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni43 – 46Cysteinyl adenylate binding4
Regioni81 – 83Cysteinyl adenylate binding3
Regioni249 – 251Cysteinyl adenylate binding3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi45 – 55"HIGH" regionAdd BLAST11
Motifi187 – 192"ERGGDP" region6
Motifi289 – 293"KMSKS" region5

Sequence similaritiesi

Phylogenomic databases

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

Family and domain databases

CDDicd00672. CysRS_core. 1 hit.
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.

A0QZY0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQSWSAPAIP VVPGRGPALR LFDSADRQVR PVTPGPTATM YVCGITPYDA
60 70 80 90 100
THLGHAATYL TFDLVHRLWL DAGHTVQYVQ NVTDVDDPLF ERAERDGIDW
110 120 130 140 150
RTLGDRETQL FREDMAALRV LPPHDYVAAT DAIAEVVEMV EKLLASGAAY
160 170 180 190 200
IVEDAEYPDV YFRADATAQF GYESGYDRDT MLTLFAERGG DPDRPGKSDQ
210 220 230 240 250
LDALLWRAER PGEPSWPSPF GRGRPGWHVE CSAIALTRIG TGLDIQGGGS
260 270 280 290 300
DLIFPHHEYS AAHAESVTGE RRFARHYVHT GMIGWDGHKM SKSRGNLVLV
310 320 330 340 350
SQLRAQGVDP SAIRLGLFSG HYREDRFWSN EVLDEANARL ARWRSATALP
360 370 380 390 400
EAPDATDVIA RVRQYLADDL DTPKALAALD GWCTDALSYG GHDTESPRLV
410
ATTVDALLGV DL
Length:412
Mass (Da):45,399
Last modified:January 9, 2007 - v1
Checksum:iF9283E2F60714E3F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK74756.1.
CP001663 Genomic DNA. Translation: AFP40549.1.
RefSeqiWP_011729628.1. NZ_CP009494.1.
YP_888468.1. NC_008596.1.

Genome annotation databases

EnsemblBacteriaiABK74756; ABK74756; MSMEG_4189.
AFP40549; AFP40549; MSMEI_4091.
GeneIDi4534157.
KEGGimsb:LJ00_20770.
msg:MSMEI_4091.
msm:MSMEG_4189.
PATRICi18080735. VBIMycSme59918_4110.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK74756.1.
CP001663 Genomic DNA. Translation: AFP40549.1.
RefSeqiWP_011729628.1. NZ_CP009494.1.
YP_888468.1. NC_008596.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3C8ZX-ray1.60A/B1-412[»]
ProteinModelPortaliA0QZY0.
SMRiA0QZY0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEG_4189.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK74756; ABK74756; MSMEG_4189.
AFP40549; AFP40549; MSMEI_4091.
GeneIDi4534157.
KEGGimsb:LJ00_20770.
msg:MSMEI_4091.
msm:MSMEG_4189.
PATRICi18080735. VBIMycSme59918_4110.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-9641.
MetaCyc:MONOMER-9682.

Miscellaneous databases

EvolutionaryTraceiA0QZY0.

Family and domain databases

CDDicd00672. CysRS_core. 1 hit.
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_MYCS2
AccessioniPrimary (citable) accession number: A0QZY0
Secondary accession number(s): I7GD10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: January 9, 2007
Last modified: November 2, 2016
This is version 74 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.