COFH_METJA
ID COFH_METJA Reviewed; 359 AA.
AC Q58826;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase;
DE EC=2.5.1.147 {ECO:0000269|PubMed:14593448, ECO:0000269|PubMed:23072415, ECO:0000269|PubMed:25781338};
DE AltName: Full=FO synthase subunit 2;
GN Name=cofH; OrderedLocusNames=MJ1431;
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 5-amino-5-(4-
CC hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-
CC ribitylamino)uracil and L-tyrosine. {ECO:0000269|PubMed:14593448,
CC ECO:0000269|PubMed:23072415, ECO:0000269|PubMed:25781338}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-
CC methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-
CC hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-
CC methionine; Xref=Rhea:RHEA:55200, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15934, ChEBI:CHEBI:17319, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:58315, ChEBI:CHEBI:59789, ChEBI:CHEBI:77846,
CC ChEBI:CHEBI:85936; EC=2.5.1.147;
CC Evidence={ECO:0000269|PubMed:14593448, ECO:0000269|PubMed:23072415,
CC ECO:0000269|PubMed:25781338};
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. CofH family.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB99441.1; -; Genomic_DNA.
DR PIR; F64478; F64478.
DR RefSeq; WP_010870949.1; NC_000909.1.
DR AlphaFoldDB; Q58826; -.
DR SMR; Q58826; -.
DR STRING; 243232.MJ_1431; -.
DR PRIDE; Q58826; -.
DR DNASU; 1452335; -.
DR EnsemblBacteria; AAB99441; AAB99441; MJ_1431.
DR GeneID; 1452335; -.
DR KEGG; mja:MJ_1431; -.
DR eggNOG; arCOG00656; Archaea.
DR HOGENOM; CLU_040406_1_1_2; -.
DR InParanoid; Q58826; -.
DR OMA; ATMMFGS; -.
DR OrthoDB; 26917at2157; -.
DR PhylomeDB; Q58826; -.
DR BioCyc; MetaCyc:MON-12179; -.
DR BRENDA; 2.5.1.147; 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:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01612; FO_synth_sub2; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR045567; CofH/MnqC-like_C.
DR InterPro; IPR019940; CofH_family.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR034405; F420.
DR InterPro; IPR020050; FO_synthase_su2.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR43076; PTHR43076; 1.
DR Pfam; PF19288; CofH_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00293; ((2_3_4_5-tetrahydroxypentyl)a; 1.
DR SFLD; SFLDF00343; aminofutalosine_synthase_(mqnE; 1.
DR SFLD; SFLDS00029; Radical_SAM; 2.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR03551; F420_cofH; 1.
DR TIGRFAMs; TIGR00423; TIGR00423; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..359
FT /note="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-
FT hydroxyphenyl transferase"
FT /id="PRO_0000141718"
FT DOMAIN 45..278
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
SQ SEQUENCE 359 AA; 40806 MW; 10B91CA7D9E18E13 CRC64;
MDPNKFREKE ISKKEALELF EDNEIIFELF KFADSLRREE VGDIVTYVVN RNINFTNICV
GNCRFCAFRA NENDKHAYFL DIDEIAKRAV EAKKFGCTEV CIQGGLHPKI DTYYQAEILK
AVHEATKPYG DIHIHAFSPM EVYFGAENAG LDIKEALKIL KENGLNSMPG TAAEILDDDI
RAELCPNKIK TKEWIYIIKE AHKLGIPTTA TMMYGHIEEY KHWVNHLFII KEIQEETNGF
TEFVPLSFMH KYAPIYKEGK AKAGATGIED LKVFAVSRII FKGLIKNIQA SWVKLGKKMV
QVALRCGAND VGGTLIEESI SRSAGAEHGV YMSVEEIRDM IKRVGLIPKE RTTLYKILE
