COFG_METMP
ID COFG_METMP Reviewed; 330 AA.
AC Q6LYV9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
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=MMP0876;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAF30432.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX950229; CAF30432.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011170820.1; NC_005791.1.
DR AlphaFoldDB; Q6LYV9; -.
DR SMR; Q6LYV9; -.
DR STRING; 267377.MMP0876; -.
DR EnsemblBacteria; CAF30432; CAF30432; MMP0876.
DR GeneID; 2761870; -.
DR KEGG; mmp:MMP0876; -.
DR PATRIC; fig|267377.15.peg.902; -.
DR eggNOG; arCOG00657; Archaea.
DR HOGENOM; CLU_054174_0_0_2; -.
DR OMA; TTACRYT; -.
DR OrthoDB; 52096at2157; -.
DR UniPathway; UPA00072; -.
DR Proteomes; UP000000590; 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..330
FT /note="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase"
FT /id="PRO_0000147767"
FT DOMAIN 13..253
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
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"
FT BINDING 31
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 34
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 330 AA; 38039 MW; F5D3AD578355AECA CRC64;
MGKINAENTS KHVTFSKNAF IPVCNWCRNV CGYCTFRNEN FKLLKMDEMK EILTKADTFG
CREALFTFGE NVDENEKVKE ELKKMGYSGI LEYLYEISAW CLENTNLIPH TNCGILSYDE
LKYLREVNAS MGLMLENSSA RLCGTIAHEK SPGKDPKLRI EMIENAGKLK IPFTTGILIG
IGETFEERVN SIFEIKRIHE KYGHIQEVIV QNFRSKPQIP MENYKEPSPV EMFKMIILSK
LILEDISIQV PPNLNRETGQ LFLMAGIDDW GGVSPLTKDF VNPEAPWPDI EELNIFSKEL
GFTLKERLPV YEKYITEEWV DKKILEKIKK
