ID   COFG_HALS3              Reviewed;         367 AA.
AC   B0R6P8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 3.
DT   03-AUG-2022, entry version 76.
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=OE_3722F;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
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; AM774415; CAP14417.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0R6P8; -.
DR   SMR; B0R6P8; -.
DR   EnsemblBacteria; CAP14417; CAP14417; OE_3722F.
DR   KEGG; hsl:OE_3722F; -.
DR   HOGENOM; CLU_054174_0_0_2; -.
DR   OMA; TTACRYT; -.
DR   PhylomeDB; B0R6P8; -.
DR   UniPathway; UPA00072; -.
DR   Proteomes; UP000001321; 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..367
FT                   /note="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase"
FT                   /id="PRO_0000335560"
FT   DOMAIN          39..275
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         53
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         57
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         60
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   367 AA;  39927 MW;  4A60364CF5795EDC CRC64;
     MTETQFGGDE YDVSVSVSEA AVERALDVRP ADVAPASSLT FARNVFVPLT TACRYTCTYC
     TYYDVPGEAS LLTPEEIREQ CRVGADAGCT EALFTFGDQP DDRYTAIHEQ LGEWGYDSIH
     EYLRAACEIA LEAGLLPHAN PGDQTRAQMA TVADVNASMG VMLETTADVQ AHGGPRAKSP
     EQRLHTIDVA GDLGVPFTTG ILVGIGEDWR DRAESLLAIR ALHERHDHVQ EVIVQPVRPN
     ARWQGEPPGA ETMRRVVAMA RAVLPAEVGV QVPPNLTDVR GLVDCGVDDL GGVSPVTKDH
     INPDYAWPAL DELSAIADHA GVPLRERLPV YERFLPADGG TADDGWVSQR IWRAIEDGDR
     YEAVRAE