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Database: UniProt
Entry: F0RDZ7_CELLC
LinkDB: F0RDZ7_CELLC
Original site: F0RDZ7_CELLC 
ID   F0RDZ7_CELLC            Unreviewed;       382 AA.
AC   F0RDZ7;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Ergothioneine biosynthesis protein EgtB {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=Celly_3135 {ECO:0000313|EMBL:ADY30952.1};
OS   Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 /
OS   NCIMB 1423 / VKM B-1433 / Cy l20).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Cellulophaga.
OX   NCBI_TaxID=867900 {ECO:0000313|EMBL:ADY30952.1, ECO:0000313|Proteomes:UP000007487};
RN   [1] {ECO:0000313|EMBL:ADY30952.1, ECO:0000313|Proteomes:UP000007487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 /
RC   VKM B-1433 / Cy l20 {ECO:0000313|Proteomes:UP000007487};
RX   PubMed=21677859; DOI=10.4056/sigs.1774329;
RA   Pati A., Abt B., Teshima H., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pagani I., Mavromatis K., Ovchinikova G., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA   Brambilla E.M., Kannan K.P., Rohde M., Spring S., Goker M., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Ivanova N.;
RT   "Complete genome sequence of Cellulophaga lytica type strain (LIM- 21).";
RL   Stand. Genomic Sci. 4:221-232(2011).
CC   -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00037882}.
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DR   EMBL; CP002534; ADY30952.1; -; Genomic_DNA.
DR   RefSeq; WP_013622695.1; NC_015167.1.
DR   AlphaFoldDB; F0RDZ7; -.
DR   STRING; 867900.Celly_3135; -.
DR   KEGG; cly:Celly_3135; -.
DR   eggNOG; COG1262; Bacteria.
DR   HOGENOM; CLU_012431_9_0_10; -.
DR   OMA; CRGTFRN; -.
DR   OrthoDB; 9768004at2; -.
DR   Proteomes; UP000007487; Chromosome.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007487}.
FT   DOMAIN          10..138
FT                   /note="DinB-like"
FT                   /evidence="ECO:0000259|Pfam:PF12867"
FT   DOMAIN          170..304
FT                   /note="Sulfatase-modifying factor enzyme"
FT                   /evidence="ECO:0000259|Pfam:PF03781"
SQ   SEQUENCE   382 AA;  45021 MW;  4947E6619986FC80 CRC64;
     MINIKSAYLN TRNQFLTLCS NLETEDYSVQ PTEFVSPPKW HLAHTTWFFE QFVLKEFSSE
     YTIYNDDFAY LFNSYYNNAG ERVLRPNRGL MTRPTVKEVY AYRNYVDSKM VVFLDSNPSK
     KALEIIELGI NHEQQHQELF YYDIKYIFGN QPTFPTLKNS IALNDITQKQ EFITIKEGVY
     QIGHNTTGFS FDNELGVHKT YLHQFKISNN LTTNAEYIAF IEAGGYSNFN LWHAEGWDFI
     TKNNITAPLY WHKVKDTWHY YTLNGFKPVE PNKPVTHISM YEAYAYAEWK QMRLPTEFEW
     EIAAEHLNYG QLWEWTNSAY LPYPNFSKAP GALGEYNGKF MINQHVLRGA SIATPENHSR
     KTYRNFFQAD MRWLFSGIRL AQ
//
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