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Database: UniProt
Entry: B6AN10_9BACT
LinkDB: B6AN10_9BACT
Original site: B6AN10_9BACT 
ID   B6AN10_9BACT            Unreviewed;       517 AA.
AC   B6AN10;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Cobalamin B12-binding/Radical SAM family protein {ECO:0000313|EMBL:EDZ39867.1};
GN   ORFNames=CGL2_11389023 {ECO:0000313|EMBL:EDZ39867.1};
OS   Leptospirillum sp. Group II '5-way CG'.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=419541 {ECO:0000313|EMBL:EDZ39867.1};
RN   [1] {ECO:0000313|EMBL:EDZ39867.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14961025; DOI=10.1038/nature02340;
RA   Tyson G.W., Chapman J., Hugenholtz P., Allen E.E., Ram R.J.,
RA   Richardson P.M., Solovyev V.V., Rubin E.M., Rokhsar D.S., Banfield J.F.;
RT   "Community structure and metabolism through reconstruction of microbial
RT   genomes from the environment.";
RL   Nature 428:37-43(2004).
RN   [2] {ECO:0000313|EMBL:EDZ39867.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18651792; DOI=10.1371/journal.pbio.0060177;
RA   Simmons S.L., Dibartolo G., Denef V.J., Goltsman D.S., Thelen M.P.,
RA   Banfield J.F.;
RT   "Population genomic analysis of strain variation in Leptospirillum group II
RT   bacteria involved in acid mine drainage formation.";
RL   PLoS Biol. 6:E177-E177(2008).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR   EMBL; DS995259; EDZ39867.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6AN10; -.
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:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01335; Radical_SAM; 1.
DR   CDD; cd02068; radical_SAM_B12_BD; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR   InterPro; IPR027564; HpnR_B12_rSAM.
DR   InterPro; IPR034466; Methyltransferase_Class_B.
DR   InterPro; IPR007197; rSAM.
DR   NCBIfam; TIGR04367; HpnR_B12_rSAM; 1.
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; SFLDF00565; hopanoid_C3-methyltransferase; 1.
DR   SFLD; SFLDG01123; methyltransferase_(Class_B); 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:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          8..141
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
FT   DOMAIN          182..396
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   517 AA;  59206 MW;  D5932E8182F4D6DE CRC64;
     MRFLAVHPSP LMYTKIYLRL EPLGLELLGA AARNAGHDVR LIDLQVENHK DYLRLISEWK
     PDAVGFSVNY LANIPEVIDL VRETRRILDN ALLFAGGHSA SFVARDMLRH AGGAMDCVLR
     GEGEASVVSL LEAWSEGPGM ISRVPGVVTS QGEGPPPRFI ENLDDIQPAR DLLRHRRKYF
     IGVLDPCASI EFARGCPWDC SFCSAWTFYG RSYRTRSPQR ILEDLERIRE PGIFIVDDVA
     FVQEKHGYEI GEAVLKKGIR KEYYLETRGD VLLRNKDLFR FWKKLGMKYM FLGVEAIDAE
     GLALHRKRIS LGKNFEALEF ARSLGITVAI NLIADPSWER ERFESIRQWC LEIPEIVNIS
     VNTPYPGTES WRTESRSLQT RDYRLFDIQH AVLPTKMPLE EFYGELVKTQ QILNKKHLGW
     QALKGTANIV ARHLMHGQTN FLRMLWKFNS VYNPALQLAD HARPVRYEMS LPPPVKEHLH
     PVTLYVHEGK GRRGRELSDT VEAFVNETRM GNPSEEL
//
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