ID A0A0Q8XFP4_9SPHN Unreviewed; 437 AA.
AC A0A0Q8XFP4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Sulfatase maturase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASE13_00870 {ECO:0000313|EMBL:KRC81018.1};
OS Sphingomonas sp. Root241.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736501 {ECO:0000313|EMBL:KRC81018.1, ECO:0000313|Proteomes:UP000051629};
RN [1] {ECO:0000313|EMBL:KRC81018.1, ECO:0000313|Proteomes:UP000051629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root241 {ECO:0000313|EMBL:KRC81018.1,
RC ECO:0000313|Proteomes:UP000051629};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC81018.1, ECO:0000313|Proteomes:UP000051629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root241 {ECO:0000313|EMBL:KRC81018.1,
RC ECO:0000313|Proteomes:UP000051629};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC {ECO:0000256|ARBA:ARBA00037882}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRC81018.1}.
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DR EMBL; LMIV01000001; KRC81018.1; -; Genomic_DNA.
DR RefSeq; WP_056610265.1; NZ_LMIV01000001.1.
DR AlphaFoldDB; A0A0Q8XFP4; -.
DR STRING; 1736501.ASE13_00870; -.
DR OrthoDB; 9768004at2; -.
DR Proteomes; UP000051629; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0052699; P:ergothioneine biosynthetic process; IEA:InterPro.
DR Gene3D; 1.20.120.450; dinb family like domain; 1.
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}.
FT DOMAIN 18..148
FT /note="DinB-like"
FT /evidence="ECO:0000259|Pfam:PF12867"
FT DOMAIN 219..337
FT /note="Sulfatase-modifying factor enzyme"
FT /evidence="ECO:0000259|Pfam:PF03781"
FT DOMAIN 361..435
FT /note="Sulfatase-modifying factor enzyme"
FT /evidence="ECO:0000259|Pfam:PF03781"
SQ SEQUENCE 437 AA; 48155 MW; D1B1F8D38DAB5958 CRC64;
MRTERDVNPA SSALASRFAA VRALTADLVA PLSDADATIQ SMDDASPAKW HLAHTTWFFE
TFVLRDHVPG YQVFDERWPF LFNSYYEAEG QRHARPRRGM LSRPSLDEIL AYREAVDSAL
LAALPDLPAS VRDLVALGCH HEEQHQELLL TDILHHFSIN PLQSAIWPGD PKVPVAMPGP
TGWIEGRTGV IEIGHDLVST GPGKTRIVSS VSTVSTGFAF DCEGPRHTEL LHPHALADRT
VTNGEWAAFI ADGGYRDPRH WLSDGWAWVQ AERIAAPLYW EQGDGGWTRF GLDGRRPVDP
AAPVTHVSFF EADAYASWAG ARLPTEFEWE AAASGHDPNG GNQLDAAGAV EPRPSAGGPA
FFGDVWEWTG SAYRPYPGFR PAEGAVGEYN GKFMSGQFVL RGGSCATPRG HVRASYRNFF
YPHQRWQFTG VRLAKDL
//
