COFG_GLOVI
ID COFG_GLOVI Reviewed; 319 AA.
AC Q7NIT2;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=gll2100;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000045; BAC90041.1; -; Genomic_DNA.
DR RefSeq; NP_925046.1; NC_005125.1.
DR RefSeq; WP_011142098.1; NC_005125.1.
DR AlphaFoldDB; Q7NIT2; -.
DR SMR; Q7NIT2; -.
DR STRING; 251221.35212667; -.
DR EnsemblBacteria; BAC90041; BAC90041; BAC90041.
DR KEGG; gvi:gll2100; -.
DR PATRIC; fig|251221.4.peg.2135; -.
DR eggNOG; COG1060; Bacteria.
DR HOGENOM; CLU_054174_0_0_3; -.
DR InParanoid; Q7NIT2; -.
DR OMA; TTACRYT; -.
DR OrthoDB; 940969at2; -.
DR PhylomeDB; Q7NIT2; -.
DR UniPathway; UPA00072; -.
DR Proteomes; UP000000557; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0044689; F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity; IBA:GO_Central.
DR GO; GO:0016841; F:ammonia-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
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..319
FT /note="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase"
FT /id="PRO_0000147756"
FT DOMAIN 6..236
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 319 AA; 34751 MW; 668F4FE4C91A25B9 CRC64;
MRERTVTYSP AFTLVPTREC FNRCGYCNFR ADRGAAWLQP AEVRALLLPL VGSGVVEILV
LSGEVHPHDP RRGEWFAMIE DICAVALELG FLPHTNCGVL SFEEMRALQQ LNVSLGLMLE
IDSNRLLGGV HRHAPSKIPA LRTAQLEWAG ALGIPFTTGL LLGIGETPAE REDTLRTIAR
LQDRHGHIQE VILQPHSPGG SQSWAGEPLG DAQLLGVVRL ARQILPAEIT IQIPPNLVGD
PVPLLEAGAR DLGGIGPVDV VNPDYAHPVV ERLGERLAAA GWRLEPRLPV YPHLDKRVAT
ALQPLLGEHR ARLCQAAVT
