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Database: UniProt
Entry: D2Q4S1_KRIFD
LinkDB: D2Q4S1_KRIFD
Original site: D2Q4S1_KRIFD 
ID   D2Q4S1_KRIFD            Unreviewed;       254 AA.
AC   D2Q4S1;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=Gamma-glutamyl-hercynylcysteine sulfoxide hydrolase {ECO:0000256|HAMAP-Rule:MF_02036};
DE            EC=3.5.1.118 {ECO:0000256|HAMAP-Rule:MF_02036};
DE   AltName: Full=Gamma-glutamyl hercynylcysteine S-oxide hydrolase {ECO:0000256|HAMAP-Rule:MF_02036};
GN   Name=egtC {ECO:0000256|HAMAP-Rule:MF_02036};
GN   OrderedLocusNames=Kfla_5161 {ECO:0000313|EMBL:ADB34176.1};
OS   Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Kribbellaceae; Kribbella.
OX   NCBI_TaxID=479435 {ECO:0000313|EMBL:ADB34176.1, ECO:0000313|Proteomes:UP000007967};
RN   [1] {ECO:0000313|Proteomes:UP000007967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC   {ECO:0000313|Proteomes:UP000007967};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Pukall R., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Kribbella flavida DSM 17836.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADB34176.1, ECO:0000313|Proteomes:UP000007967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC   {ECO:0000313|Proteomes:UP000007967};
RX   PubMed=21304701;
RA   Pukall R., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA   Cheng J.-F., Lucas S., Chen F., Nolan M., LaButti K., Pati A., Ivanova N.,
RA   Mavrommatis K., Mikhailova N., Pitluck S., Bruce D., Goodwin L., Land M.,
RA   Hauser L., Chang Y.-J., Jeffries C.D., Chen A., Palaniappan K., Chain P.,
RA   Rohde M., Goeker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.-P., Brettin T.;
RT   "Complete genome sequence of Kribbella flavida type strain (IFO 14399).";
RL   Stand. Genomic Sci. 2:186-193(2010).
CC   -!- FUNCTION: Catalyzes the hydrolysis of the gamma-glutamyl amide bond of
CC       hercynyl-gamma-L-glutamyl-L-cysteine sulfoxide to produce
CC       hercynylcysteine sulfoxide, a step in the biosynthesis pathway of
CC       ergothioneine. {ECO:0000256|HAMAP-Rule:MF_02036}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=gamma-L-glutamyl-hercynylcysteine S-oxide + H2O = L-glutamate
CC         + S-(hercyn-2-yl)-L-cysteine S-oxide; Xref=Rhea:RHEA:42684,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:82703,
CC         ChEBI:CHEBI:82706; EC=3.5.1.118; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02036};
CC   -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02036}.
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DR   EMBL; CP001736; ADB34176.1; -; Genomic_DNA.
DR   RefSeq; WP_012922730.1; NC_013729.1.
DR   AlphaFoldDB; D2Q4S1; -.
DR   STRING; 479435.Kfla_5161; -.
DR   KEGG; kfl:Kfla_5161; -.
DR   eggNOG; COG0121; Bacteria.
DR   HOGENOM; CLU_042555_3_0_11; -.
DR   OMA; RRAGPIW; -.
DR   OrthoDB; 9804310at2; -.
DR   UniPathway; UPA01014; -.
DR   Proteomes; UP000007967; Chromosome.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0052699; P:ergothioneine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01908; YafJ; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   HAMAP; MF_02036; EgtC; 1.
DR   InterPro; IPR017808; EgtC.
DR   InterPro; IPR026869; EgtC-like.
DR   InterPro; IPR032889; EgtC_Actinobacteria.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   NCBIfam; TIGR03442; ergothioneine biosynthesis protein EgtC; 1.
DR   PANTHER; PTHR43187:SF2; GAMMA-GLUTAMYL-HERCYNYLCYSTEINE SULFOXIDE HYDROLASE; 1.
DR   PANTHER; PTHR43187; GLUTAMINE AMIDOTRANSFERASE DUG3-RELATED; 1.
DR   Pfam; PF13230; GATase_4; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   3: Inferred from homology;
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|HAMAP-Rule:MF_02036};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_02036};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007967};
KW   Transferase {ECO:0000313|EMBL:ADB34176.1}.
FT   DOMAIN          2..254
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   254 AA;  27416 MW;  13B14531C3760411 CRC64;
     MCRHLAYLGP PVTLASLVLD PPHSLYEQSW TPWDMRGGGS VNADGFGLGW YVDGEPVRYR
     RNVPIWADES LPGLARSVRS GAVLAAVRNG TVGMPLMETA VAPFHRDQWF FSHNGRISGW
     PGSVAKLAET LPVTDLLTMG APVDSALLWT LILRRLDDGV PAAEAVAGVV LDVAAAAPES
     RLNVLLTDGE QLVATTWTHS LWVRQAAESL TVSSEPWARD DPSWQPVPDH SLLTATKNEC
     AVTPLAAPPM EGRQ
//
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