ID D6XU84_BACIE Unreviewed; 373 AA.
AC D6XU84;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase {ECO:0000256|ARBA:ARBA00012126};
DE EC=4.3.1.32 {ECO:0000256|ARBA:ARBA00012126};
GN OrderedLocusNames=Bsel_1865 {ECO:0000313|EMBL:ADH99370.1};
OS Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Salisediminibacterium.
OX NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH99370.1, ECO:0000313|Proteomes:UP000000271};
RN [1] {ECO:0000313|EMBL:ADH99370.1, ECO:0000313|Proteomes:UP000000271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC {ECO:0000313|Proteomes:UP000000271};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Stolz J.;
RT "Complete sequence of Bacillus selenitireducens MLS10.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-
CC dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-
CC didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine +
CC NH4(+); Xref=Rhea:RHEA:55204, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:59904, ChEBI:CHEBI:85936; EC=4.3.1.32;
CC Evidence={ECO:0000256|ARBA:ARBA00000328};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F0 biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004712}.
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DR EMBL; CP001791; ADH99370.1; -; Genomic_DNA.
DR AlphaFoldDB; D6XU84; -.
DR STRING; 439292.Bsel_1865; -.
DR KEGG; bse:Bsel_1865; -.
DR eggNOG; COG1060; Bacteria.
DR HOGENOM; CLU_054174_0_0_9; -.
DR OMA; TTACRYT; -.
DR OrthoDB; 9775764at2; -.
DR UniPathway; UPA00072; -.
DR Proteomes; UP000000271; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_01611; FO_synth_sub1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR019939; CofG_family.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR034405; F420.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR03550; F420_cofG; 1.
DR PANTHER; PTHR43076; FO SYNTHASE (COFH); 1.
DR PANTHER; PTHR43076:SF1; LIPOYL SYNTHASE 2; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00294; 7_8-didemethyl-8-hydroxy-5-dea; 1.
DR SFLD; SFLDG01388; 7_8-didemethyl-8-hydroxy-5-dea; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
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 36..274
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 373 AA; 43014 MW; B5D431FC4A903375 CRC64;
MNQTHSYWLH KATQTPLPKL MSEAFETKKQ YFASTITYSK NIFIPLTNIC KDRCSYCTFQ
RRPGDEGAEI IPEEEVMKQV YEAKRAGCTE ILITMGDKSD YFPEVRAWLN ERGFRNIIEY
TIHICKRIVT ETGLLPHTNA GVLTNHQLKN LKPYNPSMGM MLETTSERLM MPGEVHEHAP
DKWPHRRIRM IEEAGKLKIP FTTGLLVGIG ETWAERVDTL LEIKRINDQY GHIQEVIIQN
FQPKDGMDHL IDNKVGEDTM LRLCALANLM YQGEMHIQVP PNLNRDYLRK LIDAGITDFG
GVSPLTLDYI NPEAPWPAID RLREITAEKG QTLQERLPVY NKYFRPEWIS EPAWSAVQNL
KGREQLETIA PNA
//