ID E6XEJ6_CELAD Unreviewed; 385 AA.
AC E6XEJ6;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Ergothioneine biosynthesis protein EgtB {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=Celal_4081 {ECO:0000313|EMBL:ADV51324.1};
OS Cellulophaga algicola (strain DSM 14237 / IC166 / ACAM 630).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=688270 {ECO:0000313|EMBL:ADV51324.1, ECO:0000313|Proteomes:UP000008634};
RN [1] {ECO:0000313|EMBL:ADV51324.1, ECO:0000313|Proteomes:UP000008634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14237 / IC166 / ACAM 630
RC {ECO:0000313|Proteomes:UP000008634};
RX PubMed=21475589; DOI=10.4056/sigs.1543845;
RA Abt B., Lu M., Misra M., Han C., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Mavromatis K., Ovchinikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Brambilla E., Rohde M., Tindall B.J., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Cellulophaga algicola type strain (IC166).";
RL Stand. Genomic Sci. 4:72-80(2010).
CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC {ECO:0000256|ARBA:ARBA00037882}.
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DR EMBL; CP002453; ADV51324.1; -; Genomic_DNA.
DR RefSeq; WP_013552772.1; NC_014934.1.
DR AlphaFoldDB; E6XEJ6; -.
DR STRING; 688270.Celal_4081; -.
DR KEGG; cao:Celal_4081; -.
DR eggNOG; COG1262; Bacteria.
DR HOGENOM; CLU_012431_9_0_10; -.
DR OrthoDB; 9768004at2; -.
DR Proteomes; UP000008634; 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; 1.
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 9..140
FT /note="DinB-like"
FT /evidence="ECO:0000259|Pfam:PF12867"
FT DOMAIN 173..307
FT /note="Sulfatase-modifying factor enzyme"
FT /evidence="ECO:0000259|Pfam:PF03781"
SQ SEQUENCE 385 AA; 45216 MW; D82525D92FC033B4 CRC64;
MTNHELIHQF KKTRAHSVAL CAPLAPEDYN AQPVAFASPP KWHLAHITWF FEEMILKKFD
ENYVIFNKDF SYLFNSYYQT VGERATRSLR GAMTRPLIEE IYSYRSYVDK HIVALLKSKL
SLEIETLVTL GIQHEQQHQE LLLTDLKHTF SFNPLHPVYH ENFNLVQDTN KADGWLAMPE
GIYEIGHQGD GFCFDNELGR HKVFLHEYKL AKGLVTNRDF IAFIVAGGYQ EFKYWLDEGW
SWVQEENIIA PLYWIQKEGT WFNYTLAGLK PVDLDAILSH VSFYEAQAFA TFKNMRLPTE
FEWEAASEKF NWGKRWEWTY SAYLPYPNFK VADGAVGEYN GKFMINTMVL RGSSVATSEG
HERNTYRNFF HPKYRWQYTG IRLVK
//
