ID L0HDR6_METFS Unreviewed; 363 AA.
AC L0HDR6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase {ECO:0000256|HAMAP-Rule:MF_01612};
DE EC=2.5.1.147 {ECO:0000256|HAMAP-Rule:MF_01612};
DE AltName: Full=FO synthase subunit 2 {ECO:0000256|HAMAP-Rule:MF_01612};
GN Name=cofH {ECO:0000256|HAMAP-Rule:MF_01612};
GN OrderedLocusNames=Metfor_0135 {ECO:0000313|EMBL:AGB01219.1};
OS Methanoregula formicica (strain DSM 22288 / NBRC 105244 / SMSP).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX NCBI_TaxID=593750 {ECO:0000313|EMBL:AGB01219.1, ECO:0000313|Proteomes:UP000010824};
RN [1] {ECO:0000313|Proteomes:UP000010824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22288 / NBRC 105244 / SMSP
RC {ECO:0000313|Proteomes:UP000010824};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Imachi H.,
RA Tamaki H., Sekiguchi Y., Kamagata Y., Cadillo-Quiroz H., Zinder S.,
RA Liu W.-T., Woyke T.;
RT "Complete sequence of Methanoregula formicicum SMSP.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGB01219.1, ECO:0000313|Proteomes:UP000010824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22288 / NBRC 105244 / SMSP
RC {ECO:0000313|Proteomes:UP000010824};
RX PubMed=25189582;
RA Yamamoto K., Tamaki H., Cadillo-Quiroz H., Imachi H., Kyrpides N.,
RA Woyke T., Goodwin L., Zinder S.H., Kamagata Y., Liu W.T.;
RT "Complete Genome Sequence of Methanoregula formicica SMSPT, a Mesophilic
RT Hydrogenotrophic Methanogen Isolated from a Methanogenic Upflow Anaerobic
RT Sludge Blanket Reactor.";
RL Genome Announc. 2:e00870-14(2014).
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:0000256|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:0000256|HAMAP-
CC Rule:MF_01612};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_01612};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F0 biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01612}.
CC -!- SUBUNIT: The FO synthase complex consists of two subunits, CofG and
CC CofH. {ECO:0000256|HAMAP-Rule:MF_01612}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. CofH family.
CC {ECO:0000256|HAMAP-Rule:MF_01612}.
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DR EMBL; CP003167; AGB01219.1; -; Genomic_DNA.
DR AlphaFoldDB; L0HDR6; -.
DR STRING; 593750.Metfor_0135; -.
DR KEGG; mfo:Metfor_0135; -.
DR eggNOG; arCOG00656; Archaea.
DR HOGENOM; CLU_040406_1_0_2; -.
DR InParanoid; L0HDR6; -.
DR OrthoDB; 8186at2157; -.
DR UniPathway; UPA00072; -.
DR Proteomes; UP000010824; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0141093; F:5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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 NCBIfam; TIGR00423; CofH family radical SAM protein; 1.
DR NCBIfam; TIGR03551; F420_cofH; 1.
DR PANTHER; PTHR43076:SF13; 5-AMINO-6-(D-RIBITYLAMINO)URACIL--L-TYROSINE 4-HYDROXYPHENYL TRANSFERASE; 1.
DR PANTHER; PTHR43076; FO SYNTHASE (COFH); 1.
DR Pfam; PF19288; CofH_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF004762; CHP00423; 1.
DR SFLD; SFLDF00293; ((2_3_4_5-tetrahydroxypentyl)a; 1.
DR SFLD; SFLDF00343; aminofutalosine_synthase_(mqnE; 1.
DR SFLD; SFLDG01064; F420__menaquinone_cofactor_bio; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01612};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01612};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01612};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01612}; Reference proteome {ECO:0000313|Proteomes:UP000010824};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01612}; Transferase {ECO:0000256|HAMAP-Rule:MF_01612}.
FT DOMAIN 53..287
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 67
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01612"
SQ SEQUENCE 363 AA; 40331 MW; 4E35314125402694 CRC64;
MERDVKRLLD DVRGGHRMNA EEALLLFGTK GRDVWEIASA ADEVREQRAG NAVTYVRNQN
INVTNLCVNA CGFCGYSKKP GEEGIYFHDK AEIQRRAALA TERECTEICT VSGLHPDFSA
RSYTDVYRWI HEAAPGIHLH ASNPMEVAYA ARKSKMSTVE VLGAMKEAGL NSMCGTAAEI
LVDDVRQVIC KEKIPTKEWV RIVTEAHGLG IPSTATIMYG HCESEKDRVA HLAILRDIQD
ETNGFTEFVP LSFIHMNTPI YRQGKARAGA TGREDHLMVA VSRLFLDNFR NIQVSWVKEG
IKMAQIGLIA GANDLGGTVF EESISKGAGA TNTDYLDPKE MQRIAEDIGR PLRRRTTLYK
LVS
//
