COFG_METJA
ID COFG_METJA Reviewed; 358 AA.
AC Q57888;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase;
DE EC=4.3.1.32 {ECO:0000269|PubMed:14593448, ECO:0000269|PubMed:23072415, ECO:0000269|PubMed:25781338};
DE AltName: Full=FO synthase subunit 1;
GN Name=cofG; OrderedLocusNames=MJ0446;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=14593448; DOI=10.1007/s00203-003-0614-8;
RA Graham D.E., Xu H., White R.H.;
RT "Identification of the 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase
RT required for coenzyme F(420) biosynthesis.";
RL Arch. Microbiol. 180:455-464(2003).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23072415; DOI=10.1021/ja307762b;
RA Decamps L., Philmus B., Benjdia A., White R., Begley T.P., Berteau O.;
RT "Biosynthesis of F0, precursor of the F420 cofactor, requires a unique two
RT radical-SAM domain enzyme and tyrosine as substrate.";
RL J. Am. Chem. Soc. 134:18173-18176(2012).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RX PubMed=25781338; DOI=10.1021/ja513287k;
RA Philmus B., Decamps L., Berteau O., Begley T.P.;
RT "Biosynthetic versatility and coordinated action of 5'-deoxyadenosyl
RT radicals in deazaflavin biosynthesis.";
RL J. Am. Chem. Soc. 137:5406-5413(2015).
CC -!- FUNCTION: Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-
CC hydroxy-5-deazariboflavin (FO) from 5-amino-5-(4-hydroxybenzyl)-6-(D-
CC ribitylimino)-5,6-dihydrouracil. {ECO:0000269|PubMed:14593448,
CC ECO:0000269|PubMed:23072415, ECO:0000269|PubMed:25781338}.
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:0000269|PubMed:14593448};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.;
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F0 biosynthesis.
CC -!- SUBUNIT: Consists of two subunits, CofG and CofH.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. CofG family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB98436.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L77117; AAB98436.1; ALT_INIT; Genomic_DNA.
DR PIR; F64355; F64355.
DR RefSeq; WP_064496498.1; NC_000909.1.
DR AlphaFoldDB; Q57888; -.
DR SMR; Q57888; -.
DR STRING; 243232.MJ_0446; -.
DR EnsemblBacteria; AAB98436; AAB98436; MJ_0446.
DR GeneID; 1451306; -.
DR KEGG; mja:MJ_0446; -.
DR eggNOG; arCOG00657; Archaea.
DR HOGENOM; CLU_054174_0_0_2; -.
DR InParanoid; Q57888; -.
DR OMA; TTACRYT; -.
DR OrthoDB; 52096at2157; -.
DR PhylomeDB; Q57888; -.
DR BioCyc; MetaCyc:MON-12178; -.
DR BRENDA; 4.3.1.32; 3260.
DR UniPathway; UPA00072; -.
DR Proteomes; UP000000805; 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; IDA:MENGO.
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 SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR03550; F420_cofG; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome;
KW S-adenosyl-L-methionine.
FT CHAIN 1..358
FT /note="7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase"
FT /id="PRO_0000147764"
FT DOMAIN 35..275
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
SQ SEQUENCE 358 AA; 41582 MW; F10602568AEB449F CRC64;
MISREEAINF LNSTSSKDIL DKLAQINNTF KREYITYSKN VFIPLSKWCR NKCGYCIFRE
DKPSLMKPNE VKEILLKGDR LGCREALFTF GEHVDENKEI KEQLKSMGYD NILEYLYDLE
EWTLNNTSLL PHTNCGILNY DELKMLKDVN ASMGLMLENA SERLMNTIAH KHSPGKHPKL
RIEMIENAGK LKIPFTTGLL IGIGETNEEI VDSLFKIKEI HEKYGHIQEV IIQNFRAKKG
IPMENFKEPS PIKMLKVIIL AKLILDDISI QIPPNLNRET GQLFLLAGVD DWGGVSPLTR
DYVNPEAEWP EIKELREWTE ELGLKLKMRL PVYDKYISEE WLSEKVYNKI IEMGWLKE
