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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi43 – 431Zinc1 Publication
Binding sitei58 – 581Cysteinyl adenylate
Binding sitei227 – 2271Cysteinyl adenylate
Metal bindingi231 – 2311Zinc1 Publication
Metal bindingi256 – 2561Zinc1 Publication
Binding sitei283 – 2831Cysteinyl adenylate; via amide nitrogen and carbonyl oxygen

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.
MSME246196:GJ4Y-4188-MONOMER.

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi46 – 461T → V: 100-fold decrease in catalytic turnover. 1 Publication
Mutagenesisi55 – 551H → A: 40-fold decrease in catalytic turnover. 1 Publication
Mutagenesisi83 – 831T → V: Almost no effect. 1 Publication
Mutagenesisi227 – 2271W → F or H: 100-fold decrease in catalytic turnover. 1 Publication
Mutagenesisi251 – 2511D → A: 1200-fold decfrease in catalytic turnover. 1 Publication
Mutagenesisi251 – 2511D → N: 400-fold decrease in catalytic turnover. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 412412L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligasePRO_0000399827Add
BLAST

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

STRINGi246196.MSMEG_4189.

Structurei

Secondary structure

1
412
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi20 – 234Combined sources
Turni24 – 274Combined sources
Beta strandi28 – 314Combined sources
Beta strandi36 – 427Combined sources
Helixi53 – 7119Combined sources
Beta strandi75 – 828Combined sources
Helixi87 – 9610Combined sources
Helixi100 – 11718Combined sources
Beta strandi124 – 1285Combined sources
Helixi129 – 1313Combined sources
Helixi133 – 14513Combined sources
Beta strandi148 – 1514Combined sources
Beta strandi160 – 1623Combined sources
Turni168 – 1747Combined sources
Helixi178 – 18710Combined sources
Beta strandi203 – 2086Combined sources
Beta strandi222 – 2254Combined sources
Helixi227 – 23812Combined sources
Beta strandi243 – 2497Combined sources
Helixi250 – 2523Combined sources
Turni253 – 2553Combined sources
Helixi256 – 26813Combined sources
Beta strandi273 – 2808Combined sources
Helixi300 – 3056Combined sources
Helixi310 – 3189Combined sources
Helixi330 – 34718Combined sources
Helixi356 – 36712Combined sources
Helixi372 – 38918Combined sources
Beta strandi392 – 3954Combined sources
Helixi396 – 40813Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiA0QZY0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni43 – 464Cysteinyl adenylate binding
Regioni81 – 833Cysteinyl adenylate binding
Regioni249 – 2513Cysteinyl adenylate binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi45 – 5511"HIGH" regionAdd
BLAST
Motifi187 – 1926"ERGGDP" region
Motifi289 – 2935"KMSKS" region

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3C8ZX-ray1.60A/B1-412[»]
ProteinModelPortaliA0QZY0.
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.
MSME246196:GJ4Y-4188-MONOMER.

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: September 7, 2016
This is version 73 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.