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Protein

Gamma-glutamyl-hercynylcysteine sulfoxide hydrolase

Gene

egtC

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of the gamma-glutamyl amide bond of hercynyl-gamma-L-glutamyl-L-cysteine sulfoxide to produce hercynylcysteine sulfoxide, a step in the biosynthesis pathway of ergothioneine.1 Publication

Catalytic activityi

Gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O = S-(hercyn-2-yl)-L-cysteine S-oxide + L-glutamate.1 Publication

Pathwayi: ergothioneine biosynthesis

This protein is involved in the pathway ergothioneine biosynthesis, which is part of Amino-acid biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway ergothioneine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei2NucleophilePROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17986.
UniPathwayiUPA01014.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-glutamyl-hercynylcysteine sulfoxide hydrolase1 Publication (EC:3.5.1.1181 Publication)
Alternative name(s):
Gamma-glutamyl hercynylcysteine S-oxide hydrolase1 Publication
Gene namesi
Name:egtC1 Publication
Ordered Locus Names:MSMEG_6248, MSMEI_6087
OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Taxonomic identifieri246196 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000006158 Componenti: Chromosome
  • UP000000757 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004136491 – 227Gamma-glutamyl-hercynylcysteine sulfoxide hydrolaseAdd BLAST227

Interactioni

Protein-protein interaction databases

STRINGi246196.MSMEG_6248.

Structurei

Secondary structure

1227
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 13Combined sources11
Helixi14 – 18Combined sources5
Helixi25 – 28Combined sources4
Beta strandi45 – 50Combined sources6
Beta strandi56 – 63Combined sources8
Helixi65 – 67Combined sources3
Helixi69 – 74Combined sources6
Helixi75 – 77Combined sources3
Beta strandi79 – 87Combined sources9
Helixi98 – 100Combined sources3
Beta strandi104 – 108Combined sources5
Beta strandi110 – 116Combined sources7
Helixi119 – 121Combined sources3
Beta strandi129 – 132Combined sources4
Helixi133 – 144Combined sources12
Helixi146 – 148Combined sources3
Helixi149 – 159Combined sources11
Beta strandi164 – 170Combined sources7
Beta strandi172 – 182Combined sources11
Beta strandi185 – 189Combined sources5
Beta strandi192 – 198Combined sources7
Beta strandi211 – 218Combined sources8
Beta strandi221 – 226Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZFJX-ray1.75A/B/C/D/E/F/G/H/I/J/K/L1-227[»]
4ZFKX-ray1.82A/B/C/D1-227[»]
4ZFLX-ray1.70A/B/C/D/E/F/G/H/I/J/K/L2-227[»]
ProteinModelPortaliA0R5M9.
SMRiA0R5M9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 227Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd BLAST226

Sequence similaritiesi

Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiENOG4108V75. Bacteria.
COG0121. LUCA.
HOGENOMiHOG000256686.
KOiK07008.
OMAiNADGWGA.
OrthoDBiPOG091H068K.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_02036. EgtC. 1 hit.
InterProiIPR017808. EgtC.
IPR032889. EgtC_Actinobacteria.
IPR017932. GATase_2_dom.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR03442. TIGR03442. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A0R5M9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCRHVAWLGA PRSLADLVLD PPQGLLVQSY APRRQKHGLM NADGWGAGFF
60 70 80 90 100
DDEGVARRWR SDKPLWGDAS FASVAPALRS RCVLAAVRSA TIGMPIEPSA
110 120 130 140 150
SAPFSDGQWL LSHNGLVDRG VLPLTGAAES TVDSAIVAAL IFSRGLDALG
160 170 180 190 200
ATIAEVGELD PNARLNILAA NGSRLLATTW GDTLSVLHRP DGVVLASEPY
210 220
DDDPGWSDIP DRHLVDVRDA HVVVTPL
Length:227
Mass (Da):24,139
Last modified:January 9, 2007 - v1
Checksum:i715B28231359B540
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK74731.1.
CP001663 Genomic DNA. Translation: AFP42518.1.
RefSeqiWP_011731157.1. NZ_CP009494.1.
YP_890467.1. NC_008596.1.

Genome annotation databases

EnsemblBacteriaiABK74731; ABK74731; MSMEG_6248.
AFP42518; AFP42518; MSMEI_6087.
GeneIDi4532675.
KEGGimsb:LJ00_30895.
msg:MSMEI_6087.
msm:MSMEG_6248.
PATRICi18084739. VBIMycSme59918_6087.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK74731.1.
CP001663 Genomic DNA. Translation: AFP42518.1.
RefSeqiWP_011731157.1. NZ_CP009494.1.
YP_890467.1. NC_008596.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZFJX-ray1.75A/B/C/D/E/F/G/H/I/J/K/L1-227[»]
4ZFKX-ray1.82A/B/C/D1-227[»]
4ZFLX-ray1.70A/B/C/D/E/F/G/H/I/J/K/L2-227[»]
ProteinModelPortaliA0R5M9.
SMRiA0R5M9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEG_6248.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK74731; ABK74731; MSMEG_6248.
AFP42518; AFP42518; MSMEI_6087.
GeneIDi4532675.
KEGGimsb:LJ00_30895.
msg:MSMEI_6087.
msm:MSMEG_6248.
PATRICi18084739. VBIMycSme59918_6087.

Phylogenomic databases

eggNOGiENOG4108V75. Bacteria.
COG0121. LUCA.
HOGENOMiHOG000256686.
KOiK07008.
OMAiNADGWGA.
OrthoDBiPOG091H068K.

Enzyme and pathway databases

UniPathwayiUPA01014.
BioCyciMetaCyc:MONOMER-17986.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_02036. EgtC. 1 hit.
InterProiIPR017808. EgtC.
IPR032889. EgtC_Actinobacteria.
IPR017932. GATase_2_dom.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR03442. TIGR03442. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEGTC_MYCS2
AccessioniPrimary (citable) accession number: A0R5M9
Secondary accession number(s): I7FUF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: January 9, 2007
Last modified: November 2, 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.