ID A0A0N9V273_SPHMC Unreviewed; 435 AA.
AC A0A0N9V273;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Ergothioneine biosynthesis protein EgtB {ECO:0008006|Google:ProtNLM};
GN ORFNames=AN936_19180 {ECO:0000313|EMBL:ALH82399.1};
OS Sphingopyxis macrogoltabida (Sphingomonas macrogoltabidus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=33050 {ECO:0000313|EMBL:ALH82399.1, ECO:0000313|Proteomes:UP000058074};
RN [1] {ECO:0000313|EMBL:ALH82399.1, ECO:0000313|Proteomes:UP000058074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EY-1 {ECO:0000313|EMBL:ALH82399.1,
RC ECO:0000313|Proteomes:UP000058074};
RX PubMed=26634754;
RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA Tsuda M., Fujita N., Kawai F.;
RT "Complete Genome Sequence of Polypropylene Glycol- and Polyethylene Glycol-
RT Degrading Sphingopyxis macrogoltabida Strain EY-1.";
RL Genome Announc. 3:0-0(2015).
CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC {ECO:0000256|ARBA:ARBA00037882}.
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DR EMBL; CP012700; ALH82399.1; -; Genomic_DNA.
DR RefSeq; WP_054589448.1; NZ_CP012700.1.
DR AlphaFoldDB; A0A0N9V273; -.
DR KEGG; smag:AN936_19180; -.
DR PATRIC; fig|33050.5.peg.3978; -.
DR OrthoDB; 9768004at2; -.
DR Proteomes; UP000058074; 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:UP000058074}.
FT DOMAIN 24..153
FT /note="DinB-like"
FT /evidence="ECO:0000259|Pfam:PF12867"
FT DOMAIN 203..327
FT /note="Sulfatase-modifying factor enzyme"
FT /evidence="ECO:0000259|Pfam:PF03781"
FT DOMAIN 340..433
FT /note="Sulfatase-modifying factor enzyme"
FT /evidence="ECO:0000259|Pfam:PF03781"
FT REGION 333..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 435 AA; 47729 MW; 57AFD44C53951816 CRC64;
MASQNDALPL TAGTDAMLAL SGRFAATRRL SLDLVAALSD ADASAQSMPD ASPAKWHLAH
TTWFFETFVL RDHLPGYRLF DARYPYLFNS YYEAEGPRHA RPQRGLLTRP SLDEICVWRA
HVDAAVQSAL PALPLAAHAL VTLGIQHEQQ HQELLLTDIK HLFAQNPLGP AIWPTDDAIA
REVAQISAAS ADAGPMRWIK GAEGVVQIGH AGEDFAFDCE LPQFSALLTP HALASRAVSN
GEWQQFIGDG GYHTPSLWLS DGWAWVQDED IDAPAYWDGG RQFTLSGWRD IDPAAPVTHI
SFYEADAFAT WAGARLPTEI EWEAAAATFD PASGQQLDRA GPIQPAGDTS DADTDLQQMF
GSVWEWTGSA YRPYPGFRAA PGAVGEYNGK FMSGQFVLRG GSCATPRGHC RASYRNFFYP
HQRWQFTGVR LAKDL
//
