COFH2_METMA
ID COFH2_METMA Reviewed; 384 AA.
AC Q8PU53;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01612};
GN Name=cofH2 {ECO:0000255|HAMAP-Rule:MF_01612}; OrderedLocusNames=MM_2496;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM32192.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE008384; AAM32192.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011034414.1; NC_003901.1.
DR AlphaFoldDB; Q8PU53; -.
DR SMR; Q8PU53; -.
DR STRING; 192952.MM_2496; -.
DR EnsemblBacteria; AAM32192; AAM32192; MM_2496.
DR GeneID; 24882220; -.
DR GeneID; 66135457; -.
DR KEGG; mma:MM_2496; -.
DR PATRIC; fig|192952.21.peg.2857; -.
DR eggNOG; arCOG00656; Archaea.
DR HOGENOM; CLU_040406_1_0_2; -.
DR OMA; IYGHIEE; -.
DR UniPathway; UPA00072; -.
DR Proteomes; UP000000595; 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; 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 SMART; SM00729; Elp3; 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; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..384
FT /note="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-
FT hydroxyphenyl transferase 2"
FT /id="PRO_0000141721"
FT DOMAIN 53..286
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 67
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 71
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"
SQ SEQUENCE 384 AA; 42094 MW; 1643217F8D0B4D79 CRC64;
MYTKKPTIPE NVIERAYKGK CTKEDALLLL EGNPFELFEL ANDLRAIAAG DTVSYVVNRN
IYITNKCVGN CGFCAYRTEK GYILSIEEIL KKAGDARKAG AVEVCVQGGY TPEADMEFYL
EVIESLKAEY PDLCLHALSP MEVNYAAETS GMSVEEALRR LKKSGLDSLT GTSAEILSDR
VRKIICPSKI STQQWIDTVT AAHKAGISTN ATIMYGHVET LKERLDHVFT IREIQKETGG
FTELIPMSFL PYNNPVGEKM LASGKFSSTG LEDLQLIAIS RVILHTYVKN IQATWVKLGK
KLAQVALQCG ANDLGGTLME DQISTASGGS HGEYVSPAEF EWMIKGAGRV PVQRDTLYRK
IESGFPGQEG LFPGYAKAGM GSKE
