ID G7UUX0_PSEUP Unreviewed; 431 AA.
AC G7UUX0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Ergothioneine biosynthesis protein EgtB {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=DSC_01980 {ECO:0000313|EMBL:AER55049.1};
OS Pseudoxanthomonas spadix (strain BD-a59).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER55049.1, ECO:0000313|Proteomes:UP000005870};
RN [1] {ECO:0000313|EMBL:AER55049.1, ECO:0000313|Proteomes:UP000005870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD-a59 {ECO:0000313|EMBL:AER55049.1,
RC ECO:0000313|Proteomes:UP000005870};
RX PubMed=22207748; DOI=10.1128/JB.06436-11;
RA Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.;
RT "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas
RT spadix BD-a59.";
RL J. Bacteriol. 194:544-544(2012).
CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC {ECO:0000256|ARBA:ARBA00037882}.
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; CP003093; AER55049.1; -; Genomic_DNA.
DR RefSeq; WP_014159227.1; NC_016147.2.
DR AlphaFoldDB; G7UUX0; -.
DR STRING; 1045855.DSC_01980; -.
DR KEGG; psd:DSC_01980; -.
DR eggNOG; COG1262; Bacteria.
DR HOGENOM; CLU_012431_9_0_6; -.
DR OrthoDB; 9768004at2; -.
DR Proteomes; UP000005870; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0052699; P:ergothioneine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.90.1580.10; paralog of FGE (formylglycine-generating enzyme); 1.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR024775; DinB-like.
DR InterPro; IPR034660; DinB/YfiT-like.
DR InterPro; IPR017806; EgtB.
DR InterPro; IPR005532; SUMF_dom.
DR InterPro; IPR042095; SUMF_sf.
DR NCBIfam; TIGR03440; egtB_TIGR03440; 1.
DR PANTHER; PTHR23150:SF36; HERCYNINE OXYGENASE; 1.
DR PANTHER; PTHR23150; SULFATASE MODIFYING FACTOR 1, 2; 1.
DR Pfam; PF12867; DinB_2; 1.
DR Pfam; PF03781; FGE-sulfatase; 2.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF109854; DinB/YfiT-like putative metalloenzymes; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000005870}.
FT DOMAIN 25..156
FT /note="DinB-like"
FT /evidence="ECO:0000259|Pfam:PF12867"
FT DOMAIN 208..341
FT /note="Sulfatase-modifying factor enzyme"
FT /evidence="ECO:0000259|Pfam:PF03781"
FT DOMAIN 343..428
FT /note="Sulfatase-modifying factor enzyme"
FT /evidence="ECO:0000259|Pfam:PF03781"
SQ SEQUENCE 431 AA; 48330 MW; E455E4F5D765B7FA CRC64;
MHAKTPAAVA GHDLTSRTED LRARFAAMRA TTRALAAPLS AEDAMVQSMD DASPAKWHLA
HTTWFFERFI LAGDVQYRPF DPAWDYLFNS YYNSVGPMHA RPRRGLLSRP SLEQVRAYRQ
HVEARLQQRL HAHALDHAAL DILELGIQHE QQHQELLLTD IRHALWSNPL QPAYREDLPG
TRAGASPLRW IAREEQIVEI GAASWPAAKD FAYDNESPRH RALVPAHALA SRPVSNAEFQ
AFIDDGGYRT PAPWLSDGWA TVQARGWQRP LYWHQDGARE FTLGGWRERD PDAPACGLSL
FEADAFARWA GARLPTEAEW EQAATGLAVD GNFIETDALH PQSVPAAETG FAQLFGDVWE
WTGSAYLPYP GFAPWPGALG EYNGKFMNAQ WVLRGGSCAT ARNHIRASYR NFFPSDARWQ
FAGVRLAKDL T
//
