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COFG_TRIV2
ID   COFG_TRIV2              Reviewed;         340 AA.
AC   Q3MCR5;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=Ava_1598;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
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; CP000117; ABA21221.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3MCR5; -.
DR   SMR; Q3MCR5; -.
DR   STRING; 240292.Ava_1598; -.
DR   EnsemblBacteria; ABA21221; ABA21221; Ava_1598.
DR   KEGG; ava:Ava_1598; -.
DR   eggNOG; COG1060; Bacteria.
DR   HOGENOM; CLU_054174_0_0_3; -.
DR   OMA; TTACRYT; -.
DR   UniPathway; UPA00072; -.
DR   Proteomes; UP000002533; 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; S-adenosyl-L-methionine.
FT   CHAIN           1..340
FT                   /note="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase"
FT                   /id="PRO_0000291709"
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   340 AA;  38291 MW;  A4B6A78E089539DE CRC64;
     MTVAESTCAL VSTQPSIGKP TGGIATYSPA YTIVPTYECF NRCTYCNFRT DPGESSWMSL
     SAAEDIFKRL QNEQVCEILI LSGEVHPNSP KRQVWFQRIY DLCKLALTLG FLPHTNAGPL
     SFAEMQELKS VNVSMGLMLE QLTPKLLETV HRHAPSKLPE LRLQQLEWAG ELQIPFTTGL
     LLGIGETNDD CWETLEAISK LHQRYHHIQE VILQPHSPGN QQTFNAPAFN PHQLPEVIAK
     ARQILPSDIT IQIPPNLVKD ERWLLACVEA GARDLGGIGP KDEVNPDYPH LQAEELREIL
     QPAGWDLMPR LPVYPQFDGW LSGELQASVR RWRELVIGNW
 
 
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