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Database: UniProt
Entry: K9S426_9CYAN
LinkDB: K9S426_9CYAN
Original site: K9S426_9CYAN 
ID   K9S426_9CYAN            Unreviewed;       440 AA.
AC   K9S426;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Ergothioneine biosynthesis protein EgtB {ECO:0008006|Google:ProtNLM};
DE   Flags: Precursor;
GN   ORFNames=GEI7407_0023 {ECO:0000313|EMBL:AFY64529.1};
OS   Geitlerinema sp. PCC 7407.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Geitlerinematales;
OC   Geitlerinemataceae; Geitlerinema.
OX   NCBI_TaxID=1173025 {ECO:0000313|EMBL:AFY64529.1, ECO:0000313|Proteomes:UP000010383};
RN   [1] {ECO:0000313|EMBL:AFY64529.1, ECO:0000313|Proteomes:UP000010383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7407 {ECO:0000313|EMBL:AFY64529.1,
RC   ECO:0000313|Proteomes:UP000010383};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished genome of Geitlerinema sp. PCC 7407.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00037882}.
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DR   EMBL; CP003591; AFY64529.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9S426; -.
DR   STRING; 1173025.GEI7407_0023; -.
DR   KEGG; gei:GEI7407_0023; -.
DR   PATRIC; fig|1173025.3.peg.26; -.
DR   eggNOG; COG1262; Bacteria.
DR   HOGENOM; CLU_012431_9_2_3; -.
DR   Proteomes; UP000010383; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.450; dinb family like domain; 1.
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; IPR005532; SUMF_dom.
DR   InterPro; IPR042095; SUMF_sf.
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:UP000010383}.
FT   DOMAIN          39..161
FT                   /note="DinB-like"
FT                   /evidence="ECO:0000259|Pfam:PF12867"
FT   DOMAIN          188..433
FT                   /note="Sulfatase-modifying factor enzyme"
FT                   /evidence="ECO:0000259|Pfam:PF03781"
SQ   SEQUENCE   440 AA;  49886 MW;  C1A80B2083EBC1BD CRC64;
     MKFNITPSNS ATSGSATSGS ATAIAPLAHR RDALRQDLID ARRATLAIFE GIDAATFCYH
     AHPDFSPVGW HLGHIGFTEA LWLLEPRGVG DFLTPERRRL YAADGLPKAA RAQLPTLAQT
     VDFLEAVRQA TLETLEQVSL ESEERLWRWL LQHEAQHSET IRIVLQIQRW PEGAPTVAKG
     DRTVPPSEDM VAIPGGSFEM GSGAIAAIDN ERPSHRVQVE PYWLDRAPVT VAQYRHFIAA
     GGYETERWWH PEGWAWRQAA QIRRPRYWSN DPCWDDHPVC GVSWYEADAY ARFAHKRLPT
     EAEWERAARW QAFSQSGEAG PLYPWGEAQP APQHANFQGY QGQTTPVGTY PASGAGCHDL
     LGNVWEWTNT WFAPYAGFEA YPYRGYSQAY FDQQHRVLRG GSWATPRWTL RSSFRNWYHP
     SVREIFAGFR CARDPSPQRK
//
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