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Database: UniProt
Entry: A0A097EI89_9SPHN
LinkDB: A0A097EI89_9SPHN
Original site: A0A097EI89_9SPHN 
ID   A0A097EI89_9SPHN        Unreviewed;       416 AA.
AC   A0A097EI89;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Ergothioneine biosynthesis protein EgtB {ECO:0008006|Google:ProtNLM};
GN   ORFNames=MC45_13970 {ECO:0000313|EMBL:AIT07295.1};
OS   Sphingomonas taxi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1549858 {ECO:0000313|EMBL:AIT07295.1, ECO:0000313|Proteomes:UP000033200};
RN   [1] {ECO:0000313|EMBL:AIT07295.1, ECO:0000313|Proteomes:UP000033200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55669 {ECO:0000313|EMBL:AIT07295.1,
RC   ECO:0000313|Proteomes:UP000033200};
RA   Zhou Y., Ma T., Liu T.;
RT   "Using Illumina technology Improving SMRT sequencing Genome Assembly by
RT   RASTools.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00037882}.
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DR   EMBL; CP009571; AIT07295.1; -; Genomic_DNA.
DR   RefSeq; WP_038664360.1; NZ_CP009571.1.
DR   AlphaFoldDB; A0A097EI89; -.
DR   STRING; 1549858.MC45_13970; -.
DR   KEGG; stax:MC45_13970; -.
DR   eggNOG; COG1262; Bacteria.
DR   HOGENOM; CLU_012431_9_0_5; -.
DR   Proteomes; UP000033200; 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); 2.
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:UP000033200}.
FT   DOMAIN          16..145
FT                   /note="DinB-like"
FT                   /evidence="ECO:0000259|Pfam:PF12867"
FT   DOMAIN          181..327
FT                   /note="Sulfatase-modifying factor enzyme"
FT                   /evidence="ECO:0000259|Pfam:PF03781"
FT   DOMAIN          341..414
FT                   /note="Sulfatase-modifying factor enzyme"
FT                   /evidence="ECO:0000259|Pfam:PF03781"
FT   REGION          314..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   416 AA;  46188 MW;  17A962C99282125A CRC64;
     MLKIAPQPLT PLAERFSAVR ALTLALAAPL SDADATVQSM PDASPTKWHL AHTTWFFETF
     VLRDHVSGYR LHDERFPFLF NSYYEAEGRR HARDRRGMIT RPTLDEVRAY RAYVDAALAA
     ALPDLPEAAR ELVALGCHHE EQHQELLVTD VLHLFGENPL EPAIWPAAPK VPVAMPGPVR
     WIDHPGGIVR IGHDGDGFAF DCEGPRHDAL LAPHALADRT VTNGEWAAFI ADGGYRDPAH
     WLADGWAWVK AEGIVAPLYW EERDGKWTRF GLDGRRAIDP AAPVTHVSLY EADAYASWAG
     ARLPTEFEWE AAAQAQDARG GNQMDAAGPV EPRPASGPAF FGDVWEWTGS AYRPYPGFRT
     IEGAVGEYNG KFMSGQFVLR GGSCATPRGH ARASYRNFFY PHQRWQFTGV RLAKDL
//
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