ID   COFG_METMJ              Reviewed;         331 AA.
AC   A3CWL4;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase {ECO:0000255|HAMAP-Rule:MF_01611};
DE            EC=4.3.1.32 {ECO:0000255|HAMAP-Rule:MF_01611};
DE   AltName: Full=FO synthase subunit 1 {ECO:0000255|HAMAP-Rule:MF_01611};
GN   Name=cofG {ECO:0000255|HAMAP-Rule:MF_01611}; OrderedLocusNames=Memar_1838;
OS   Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=368407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX   PubMed=21304656; DOI=10.4056/sigs.32535;
RA   Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA   Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT   type strain JR1.";
RL   Stand. Genomic Sci. 1:189-196(2009).
CC   -!- FUNCTION: Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-
CC       hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D-
CC       ribitylimino)-5,6-dihydrouracil. {ECO:0000255|HAMAP-Rule:MF_01611}.
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:0000255|HAMAP-Rule:MF_01611};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01611};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000255|HAMAP-Rule:MF_01611};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme F0 biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01611}.
CC   -!- SUBUNIT: Consists of two subunits, CofG and CofH. {ECO:0000255|HAMAP-
CC       Rule:MF_01611}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. CofG family.
CC       {ECO:0000255|HAMAP-Rule:MF_01611}.
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DR   EMBL; CP000562; ABN57764.1; -; Genomic_DNA.
DR   RefSeq; WP_011844673.1; NC_009051.1.
DR   AlphaFoldDB; A3CWL4; -.
DR   STRING; 368407.Memar_1838; -.
DR   EnsemblBacteria; ABN57764; ABN57764; Memar_1838.
DR   GeneID; 4847531; -.
DR   KEGG; mem:Memar_1838; -.
DR   eggNOG; arCOG00657; Archaea.
DR   HOGENOM; CLU_054174_0_0_2; -.
DR   OMA; TTACRYT; -.
DR   OrthoDB; 52096at2157; -.
DR   UniPathway; UPA00072; -.
DR   Proteomes; UP000002146; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016841; F:ammonia-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01611; FO_synth_sub1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR019939; CofG_family.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR034405; F420.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR43076; PTHR43076; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDF00294; 7_8-didemethyl-8-hydroxy-5-dea; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR03550; F420_cofG; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; S-adenosyl-L-methionine.
FT   CHAIN           1..331
FT                   /note="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase"
FT                   /id="PRO_0000291713"
FT   DOMAIN          6..244
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         20
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01611"
FT   BINDING         24
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01611"
FT   BINDING         27
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01611"
SQ   SEQUENCE   331 AA;  36135 MW;  50B3C02E05C7627A CRC64;
     MHRRVITFSK NAFLPLTTVC QNRCGYCCFR TPVREGCVMA PTEAIRTLEA SAALGCTEAL
     FTFGERPGAV PGFNEMLGRL GYADILDYVY HLSLAAIERD LLPHTNAGIL TYAELDRLRE
     VNASMGLMLE TTADVPAHRN SPGKDPAVRI EMIENAGKLS IPFTTGILLG IGETEDDREE
     SLRVIADLHR RYGHIQEVIV QNFCPKPGTA MEGAAVPGPD EIGAAISLAR EILPADVAVQ
     IPPNLADASR LIGCGVNDLG GVSPLTIDYV NPEHPWPQLD ELRRIAGDAE LRERLCIYPQ
     YIEKGRYSPL LEPLIRRLAE RIAAPGRDAG A