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
//