ID EGTB_MYCTU Reviewed; 425 AA. AC O69671; L0TDB1; DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 10-MAY-2017, entry version 100. DE RecName: Full=Hercynine oxygenase; DE EC=1.14.99.50 {ECO:0000250|UniProtKB:A0R5N0}; DE AltName: Full=Gamma-glutamyl hercynylcysteine S-oxide synthase {ECO:0000250|UniProtKB:A0R5N0}; GN Name=egtB; OrderedLocusNames=Rv3703c; OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=83332; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the RT complete genome sequence."; RL Nature 393:537-544(1998). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=21969609; DOI=10.1074/mcp.M111.011627; RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., RA Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H., RA Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., RA Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S., RA Dash D., Pandey A.; RT "Proteogenomic analysis of Mycobacterium tuberculosis by high RT resolution mass spectrometry."; RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011). CC -!- FUNCTION: Catalyzes the oxidative sulfurization of hercynine (N- CC alpha,N-alpha,N-alpha-trimethyl-L-histidine) into hercynyl-gamma- CC L-glutamyl-L-cysteine sulfoxide, a step in the biosynthesis CC pathway of ergothioneine. Ergothioneine is an antioxidant that CC protects mycobacteria from oxidative stress. CC {ECO:0000250|UniProtKB:A0R5N0, ECO:0000250|UniProtKB:Q7D513}. CC -!- CATALYTIC ACTIVITY: Hercynine + gamma-L-glutamyl-L-cysteine + O(2) CC = gamma-L-glutamyl-S-hercyn-2-yl-L-cysteine S-oxide + H(2)O. CC {ECO:0000250|UniProtKB:A0R5N0}. CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000250|UniProtKB:A0R5N0}; CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis. CC {ECO:0000250|UniProtKB:A0R5N0}. CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:A0R5N0}. CC -!- SIMILARITY: Belongs to the EgtB family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL123456; CCP46528.1; -; Genomic_DNA. DR PIR; H70793; H70793. DR RefSeq; NP_218220.1; NC_000962.3. DR RefSeq; WP_003419808.1; NZ_KK339374.1. DR ProteinModelPortal; O69671; -. DR SMR; O69671; -. DR STRING; 83332.Rv3703c; -. DR PaxDb; O69671; -. DR EnsemblBacteria; CCP46528; CCP46528; Rv3703c. DR GeneID; 885128; -. DR KEGG; mtu:Rv3703c; -. DR PATRIC; 18156840; VBIMycTub87468_4127. DR TubercuList; Rv3703c; -. DR eggNOG; ENOG4105E46; Bacteria. DR eggNOG; COG1262; LUCA. DR HOGENOM; HOG000253478; -. DR InParanoid; O69671; -. DR KO; K18912; -. DR OMA; WEKAASW; -. DR PhylomeDB; O69671; -. DR UniPathway; UPA01014; -. DR Proteomes; UP000001584; Chromosome. DR GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB. DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB. DR GO; GO:0052704; P:ergothioneine biosynthesis from histidine via N-alpha,N-alpha,N-alpha-trimethyl-L-histidine; ISS:UniProtKB. DR HAMAP; MF_02035; EgtB; 1. DR InterPro; IPR016187; CTDL_fold. DR InterPro; IPR024775; DinB-like. DR InterPro; IPR034660; DinB/YfiT-like. DR InterPro; IPR017806; EgtB. DR InterPro; IPR032890; EgtB_Actinobacteria. DR InterPro; IPR005532; SUMF_dom. DR Pfam; PF12867; DinB_2; 1. DR Pfam; PF03781; FGE-sulfatase; 1. DR SUPFAM; SSF109854; SSF109854; 1. DR SUPFAM; SSF56436; SSF56436; 1. DR TIGRFAMs; TIGR03440; egtB_TIGR03440; 1. PE 1: Evidence at protein level; KW Complete proteome; Iron; Metal-binding; Monooxygenase; Oxidoreductase; KW Reference proteome. FT CHAIN 1 425 Hercynine oxygenase. FT /FTId=PRO_0000413648. FT REGION 82 85 Gamma-glutamylcysteine binding. FT {ECO:0000250|UniProtKB:G7CFI3}. FT METAL 46 46 Iron; via tele nitrogen. FT {ECO:0000250|UniProtKB:G7CFI3}. FT METAL 129 129 Iron; via tele nitrogen. FT {ECO:0000250|UniProtKB:G7CFI3}. FT METAL 133 133 Iron; via tele nitrogen. FT {ECO:0000250|UniProtKB:G7CFI3}. FT BINDING 408 408 Gamma-glutamylcysteine. FT {ECO:0000250|UniProtKB:G7CFI3}. FT BINDING 412 412 Gamma-glutamylcysteine. FT {ECO:0000250|UniProtKB:G7CFI3}. SQ SEQUENCE 425 AA; 47139 MW; D8CB6CB0C41E39CD CRC64; MTSPEQLACH LARARARTLR LVDFDDAELC CQYDPLMSPL VWDLAHIGQQ EELWLLRGGD PGQPGLLPPA VEGLYDAFEH SRASRVELPL LSPARARSYC ATVRSAALDA LAALPEDGDS FVFAMVISHE NQHDETMLQA LNLRTGSPLL AATSALPAGR PRMAGTSVLV AGGPFVLGVD AADEPCSLDN ERPAHVVDVP AFRIGRVPVT NGEWQDFIDD GGYTQSRWWS ERGWQHRQRA GLTAPQFWRS GGRTRTRFGH VEDIPADEPV QHVSYFEAEA YAAWAGARLP TEVEWEKACA WDPATGSRRR YPWGTEEPTD TYANLGGQTL RPAPVGAYPA GASACGAEQM LGDVWEWTTS PLRPWPGFVP MVYERYSQPF FGGDYRVLRG GSWAVEPAIL RPSFRNWDHP YRRQIFAGVR LAWDI //