FBIC_MYCLE
ID FBIC_MYCLE Reviewed; 863 AA.
AC Q9CBX6;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=FO synthase;
DE Includes:
DE RecName: Full=7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase;
DE EC=4.3.1.32;
DE Includes:
DE RecName: Full=5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase;
DE EC=2.5.1.147;
GN Name=fbiC; OrderedLocusNames=ML1492;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- FUNCTION: Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-
CC hydroxy-5-deazariboflavin (FO) from 5-amino-6-(D-ribitylamino)uracil
CC and L-tyrosine.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-
CC dihydrouracil + S-adenosyl-L-methionine = 5'-deoxyadenosine + 7,8-
CC didemethyl-8-hydroxy-5-deazariboflavin + H(+) + L-methionine +
CC NH4(+); Xref=Rhea:RHEA:55204, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:59904, ChEBI:CHEBI:85936; EC=4.3.1.32;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 2 [4Fe-4S] clusters. The clusters are coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F0 biosynthesis.
CC -!- SIMILARITY: In the N-terminal section; belongs to the radical SAM
CC superfamily. CofG family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the radical SAM
CC superfamily. CofH family. {ECO:0000305}.
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DR EMBL; AL583922; CAC30442.1; -; Genomic_DNA.
DR PIR; E87095; E87095.
DR RefSeq; NP_302048.1; NC_002677.1.
DR AlphaFoldDB; Q9CBX6; -.
DR SMR; Q9CBX6; -.
DR STRING; 272631.ML1492; -.
DR EnsemblBacteria; CAC30442; CAC30442; CAC30442.
DR KEGG; mle:ML1492; -.
DR PATRIC; fig|272631.5.peg.2800; -.
DR Leproma; ML1492; -.
DR eggNOG; COG1060; Bacteria.
DR HOGENOM; CLU_010522_1_0_11; -.
DR OMA; HWVGHLN; -.
DR UniPathway; UPA00072; -.
DR Proteomes; UP000000806; 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:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 2.
DR HAMAP; MF_01611; FO_synth_sub1; 1.
DR HAMAP; MF_01612; FO_synth_sub2; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR019939; CofG_family.
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; 2.
DR Pfam; PF19288; CofH_C; 1.
DR Pfam; PF04055; Radical_SAM; 2.
DR SFLD; SFLDF00293; ((2_3_4_5-tetrahydroxypentyl)a; 1.
DR SFLD; SFLDF00294; 7_8-didemethyl-8-hydroxy-5-dea; 1.
DR SFLD; SFLDF00343; aminofutalosine_synthase_(mqnE; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR03550; F420_cofG; 1.
DR TIGRFAMs; TIGR03551; F420_cofH; 1.
DR TIGRFAMs; TIGR00423; TIGR00423; 1.
DR PROSITE; PS51918; RADICAL_SAM; 2.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..863
FT /note="FO synthase"
FT /id="PRO_0000147770"
FT DOMAIN 91..343
FT /note="Radical SAM core 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DOMAIN 551..792
FT /note="Radical SAM core 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT REGION 92..424
FT /note="CofG-like"
FT REGION 528..861
FT /note="CofH-like"
FT BINDING 105
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 565
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 569
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 572
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
SQ SEQUENCE 863 AA; 94360 MW; 7DFD519DBC19EF86 CRC64;
MWGSYTKVSL IESQEPIALS RPVVPPKPNT SALRRVLRRA RDGFALNIDE AVVAMTARGE
DLADLCASAA RVRDVGLETA GRRGADGRLP ITYSRKVFIP VTHLCRDSCH YCTFVTAPDM
LRTQGAGMYL EPNEILNLAR RGSELGCKEA LFTLGDRPED RWAQARDWLA ERGYDSTLSY
LRAMAIRVLE ETGLLPHLNP GVMSWSELSR LKPVAPSMGM MLETTSRRLF ETKGLAHYGS
LDKDPTVRLR VLTDAGRLSI PFTTGLLVGI GETLAERADT LHEIRKSNKE FGHVQEVIVQ
NFRAKEHTAM AAVPDARIED YLATVAVARL VLGPAMRIQA PPNLVSREEC LALVTAGVDD
WGGVSPLTPD HVNPERPWPA LHELAAVTAE AGYTLVQRLT AQPKYVQAGA AWIDPRVRGH
VVALADPVTG LARDVNPVGM PWQEPDDVES AGRMDINTAI DTEGRNTEAR SDLDSAFGDW
ESIRAHVHEL ADCAPERIDT DVLAALRSAE RDPAGCTDDE YLALATADGP ALEAVTALAD
SLRRDVVGDD VTFVVNRNIN FTNICYTGCR FCAFAQRKGD TDAYSLSREE VAERAWEAHV
QGATEVCMQG GIDPELPVTG YVDLVRAVKT RVPSMHVHAF SPMEIANGVA KSGFSIREWL
ISLREAGLDT IPGTAAEILD DEVRWVLTKG KLPTSMWIEI VTTAHEVGLR SSSTMMYGHV
DGPRHWVAHL QVLRDIQDRT GGFTEFVPLP FVHQNSPLYL AGAARPGPTH RDNRAVHALA
RIMLHGRISH IQTSWVKLGV ERTQAMLNGG ANDLGGTLME ETISRMAGSE YGSAKTVAEL
IAIAEGIGRT ARQRTTTYAL RGA
