COFH_METMJ
ID COFH_METMJ Reviewed; 367 AA.
AC A3CRI3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase {ECO:0000255|HAMAP-Rule:MF_01612};
DE EC=2.5.1.147 {ECO:0000255|HAMAP-Rule:MF_01612};
DE AltName: Full=FO synthase subunit 2 {ECO:0000255|HAMAP-Rule:MF_01612};
GN Name=cofH {ECO:0000255|HAMAP-Rule:MF_01612}; OrderedLocusNames=Memar_0048;
OS Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=368407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX PubMed=21304656; DOI=10.4056/sigs.32535;
RA Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT type strain JR1.";
RL Stand. Genomic Sci. 1:189-196(2009).
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:0000255|HAMAP-Rule:MF_01612}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01612};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01612};
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_01612};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F0 biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01612}.
CC -!- SUBUNIT: Consists of two subunits, CofG and CofH. {ECO:0000255|HAMAP-
CC Rule:MF_01612}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. CofH family.
CC {ECO:0000255|HAMAP-Rule:MF_01612}.
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DR EMBL; CP000562; ABN55983.1; -; Genomic_DNA.
DR RefSeq; WP_011842904.1; NC_009051.1.
DR AlphaFoldDB; A3CRI3; -.
DR SMR; A3CRI3; -.
DR STRING; 368407.Memar_0048; -.
DR PRIDE; A3CRI3; -.
DR EnsemblBacteria; ABN55983; ABN55983; Memar_0048.
DR GeneID; 4846600; -.
DR KEGG; mem:Memar_0048; -.
DR eggNOG; arCOG00656; Archaea.
DR HOGENOM; CLU_040406_1_1_2; -.
DR OMA; ATMMFGS; -.
DR OrthoDB; 26917at2157; -.
DR UniPathway; UPA00072; -.
DR Proteomes; UP000002146; 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; IEA:UniProtKB-EC.
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; 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 TIGRFAMs; TIGR03551; F420_cofH; 1.
DR TIGRFAMs; TIGR00423; TIGR00423; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..367
FT /note="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-
FT hydroxyphenyl transferase"
FT /id="PRO_1000215709"
FT DOMAIN 56..290
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 70
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_01612"
FT BINDING 74
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_01612"
FT BINDING 77
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_01612"
SQ SEQUENCE 367 AA; 40730 MW; 1404400F39BB82E1 CRC64;
MKCMPPPLRE ILDDVLAGHR LTEEEAVRLL ATRDRGVWEI AAAANELRER KVGNVVTYVR
NQNINVTNLC VNACGFCGFS RKPGDADAFF YGETAVRGKA REARERGVTE VCTVSGLHPE
FDVQSYAEIY SWIRDEVPGV HIHASNPMEV AYAARRSGIS TREVMELMRG AGLSTLCGTA
AEILVDDVRR VICPDKIDTG SWARIIREAH GLGIRSTATI MYGHCESEAD RARHLNILRE
IQDETHGFTE FVPLSFIHKN TPLYRAGLAR AGATGREDLL MFAVARLFLD NFDHIQASWV
KVGTKMAEMA LLSGADDLGG TLFEESISRE AGARDTDYLD PAEMRRMAED LGRVLRQRTT
TYALLPG
