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Database: UniProt
Entry: A0A1G2F5I1_9BACT
LinkDB: A0A1G2F5I1_9BACT
Original site: A0A1G2F5I1_9BACT 
ID   A0A1G2F5I1_9BACT        Unreviewed;       474 AA.
AC   A0A1G2F5I1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OGZ33187.1};
GN   ORFNames=A2V69_01515 {ECO:0000313|EMBL:OGZ33187.1};
OS   Candidatus Portnoybacteria bacterium RBG_13_40_8.
OC   Bacteria; Candidatus Portnoybacteria.
OX   NCBI_TaxID=1801990 {ECO:0000313|EMBL:OGZ33187.1, ECO:0000313|Proteomes:UP000177810};
RN   [1] {ECO:0000313|EMBL:OGZ33187.1, ECO:0000313|Proteomes:UP000177810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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:OGZ33187.1}.
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DR   EMBL; MHMT01000003; OGZ33187.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2F5I1; -.
DR   STRING; 1801990.A2V69_01515; -.
DR   Proteomes; UP000177810; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd01335; Radical_SAM; 1.
DR   CDD; cd02068; radical_SAM_B12_BD; 1.
DR   Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR   Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR   InterPro; IPR034466; Methyltransferase_Class_B.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   PANTHER; PTHR43409; ANAEROBIC MAGNESIUM-PROTOPORPHYRIN IX MONOMETHYL ESTER CYCLASE-RELATED; 1.
DR   PANTHER; PTHR43409:SF17; MG-PROTOPORPHYRIN IX MONOMETHYL ESTER OXIDATIVE CYCLASE 66KD SUBUNIT; 1.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDG01123; methyltransferase_(Class_B); 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00022485};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022485}.
FT   DOMAIN          3..141
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
FT   DOMAIN          192..414
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   474 AA;  54709 MW;  2ED0182D2510E3C7 CRC64;
     MREGKVLLIV HDIYQEDNYL PLGYAYMAAV LKKEGFNVGI CCQDVFHYSN EELANLFLKN
     EDYDLIGVGF LAARFKETVL GLCNTINKYK KNAWLVLGGP GPSPIPGYVL KETKADIIAI
     GEAEETIVDL LKCKINGSDL SKVKGIAYRK NGKIIINERR EPIRDLDSIP FPDWSLFPMD
     KYTTCLKLFR GTKDDKTLDI LTGRGCINRC NFCYRMEKGI RFRSVKNVIK EILLLNSKYG
     VNYFLMGDEL FVFSKKRIFE FRDALKKNNL KIKFSCNARV DIFDEEIVNS LKESGCQFIN
     FGMESSDQRV LDLMNKNTRV EQNIMAAEIT NKAGVGLGLN FIWGNKGDTE ESLKNNVKLI
     KKYNLYDQIR TIRPVTPYPG SDLYYEAIDR GLLSGPEDFF NKFKNSDLLT VNFTDIPKEK
     FYKLLYEANK ELITDHFMHT TKDMNNANRL IKSFYDLYFK EKINFRGARH YVKK
//
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