COFH1_METAC
ID COFH1_METAC Reviewed; 375 AA.
AC Q8TQQ0;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01612};
GN Name=cofH1 {ECO:0000255|HAMAP-Rule:MF_01612}; OrderedLocusNames=MA_1490;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(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}.
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DR EMBL; AE010299; AAM04904.1; -; Genomic_DNA.
DR RefSeq; WP_011021504.1; NC_003552.1.
DR AlphaFoldDB; Q8TQQ0; -.
DR SMR; Q8TQQ0; -.
DR STRING; 188937.MA_1490; -.
DR EnsemblBacteria; AAM04904; AAM04904; MA_1490.
DR GeneID; 1473378; -.
DR KEGG; mac:MA_1490; -.
DR HOGENOM; CLU_040406_1_0_2; -.
DR InParanoid; Q8TQQ0; -.
DR OMA; ATMMFGS; -.
DR OrthoDB; 26917at2157; -.
DR PhylomeDB; Q8TQQ0; -.
DR UniPathway; UPA00072; -.
DR Proteomes; UP000002487; 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; IBA:GO_Central.
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; 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..375
FT /note="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-
FT hydroxyphenyl transferase 1"
FT /id="PRO_0000141717"
FT DOMAIN 50..284
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 64
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 68
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"
SQ SEQUENCE 375 AA; 41978 MW; 626C4C4D3B6DFB33 CRC64;
MNSKIPEDLM ERAYQGKCTK EDALQLLEVP PFELFRFADE LRDLAVGDTV TYVVNRNINF
TSRCVGTCGF CAFRTNNGKV LSIEEIMEKV RDAEKANATE VCIQGGLLPE VGLDFYQGIA
EAIKAEFPEM HIHSFSPMEV YHASRISEIP VKEALRRLKR SGLDTMPGTA AEILSDRVRK
IICPSKLKTA EWVEVVRQAH AAGIPTTATM MYGHVETREE RIDHMLIIRD IQKETGGITE
FVPLPFMPYN NPVGEKMIRE GRYATPGLED LKIYAVSRIL FHGHVDNIQA SWVKLGKKLA
QFSLHCGTND LGGTLMEESI SRSAGACHGE MITVDELEWM IHGAGRIPKE RTTLYRRVEL
ASGNLRKISG CGAYE
