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COFG_NOSS1
ID   COFG_NOSS1              Reviewed;         339 AA.
AC   Q8YR77;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=alr3573;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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; BA000019; BAB75272.1; -; Genomic_DNA.
DR   PIR; AF2252; AF2252.
DR   AlphaFoldDB; Q8YR77; -.
DR   SMR; Q8YR77; -.
DR   STRING; 103690.17132706; -.
DR   EnsemblBacteria; BAB75272; BAB75272; BAB75272.
DR   KEGG; ana:alr3573; -.
DR   eggNOG; COG1060; Bacteria.
DR   OMA; TTACRYT; -.
DR   UniPathway; UPA00072; -.
DR   Proteomes; UP000002483; 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   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; Reference proteome;
KW   S-adenosyl-L-methionine.
FT   CHAIN           1..339
FT                   /note="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase"
FT                   /id="PRO_0000147755"
FT   DOMAIN          25..256
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         39
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         43
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         46
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   339 AA;  38248 MW;  A656E1432DDF69A8 CRC64;
     MTVAKSTCAS VSTKPAVGKP TNGIATYSPA YTIVPTYECF NRCTYCNFRT DPGESSWMTL
     SAAEDIFQRL QNEQVCEILI LSGEVHPHSP KRQAWFQRIY DLCKLALTSG FLPHTNAGPL
     SFAEMQELKS VNVSMGLMLE QLTPKLLETV HRHAPSKLPE LRLQQLEWAG DLQIPFTTGL
     LLGIGEGIDD CWETLETISK LHQRYHHIQE VILQPHSPGN QQTFDAPAFN PHQLPEVIAK
     ARQILPPDIT IQIPPNLVQD EQWLVACVEA GARDLGGIGP KDEVNPDYPH LQAEELREIL
     QPVGWELVPR LPVYPQFDGW LSKELQASVR RWRELVIYF
 
 
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