COFG_METB6
ID COFG_METB6 Reviewed; 329 AA.
AC A7IAF4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
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=Mboo_2201;
OS Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX NCBI_TaxID=456442;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21154 / JCM 14090 / 6A8;
RX PubMed=25998264; DOI=10.1099/mic.0.000117;
RA Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT peatland environments.";
RL Microbiology 161:1572-1581(2015).
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; CP000780; ABS56715.1; -; Genomic_DNA.
DR RefSeq; WP_012107775.1; NC_009712.1.
DR AlphaFoldDB; A7IAF4; -.
DR SMR; A7IAF4; -.
DR STRING; 456442.Mboo_2201; -.
DR EnsemblBacteria; ABS56715; ABS56715; Mboo_2201.
DR GeneID; 5411221; -.
DR KEGG; mbn:Mboo_2201; -.
DR eggNOG; arCOG00657; Archaea.
DR HOGENOM; CLU_054174_0_0_2; -.
DR OMA; TTACRYT; -.
DR OrthoDB; 52096at2157; -.
DR UniPathway; UPA00072; -.
DR Proteomes; UP000002408; 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; Reference proteome;
KW S-adenosyl-L-methionine.
FT CHAIN 1..329
FT /note="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase"
FT /id="PRO_1000069447"
FT DOMAIN 6..244
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 329 AA; 36711 MW; 1BF7894BDDC27D04 CRC64;
MEPRVITYTK NVFLPLTSVC RNRCGYCSFR TPVQEGCVML PEEVEAVLAQ GQAAGCTEAL
FTFGEHPEEE EGFRAYLEKT GYDTILDYCE AMCRLALRYG ILPHTNAGIL TYDEMKRLRP
TNASMGLMLE TTARIPAHQG SKGKEPEVRL AMMEDAGRLK IPFTTGLLLG IGETAAGRED
SLIAIRDIHK KYGHIQEIIL QNFCPKNNTP MAAFRVPDTQ EICNTILMAR RILPEEISIQ
VAPNLIDASR LIGCGVSDLG GISPVTIDYV NPEHPWPAFN DLKKIVGDAT LQERLCIYPR
FIRPGWYDPG LQPLINRLNQ RISRGSSQP
