FBIC_NOCFA
ID FBIC_NOCFA Reviewed; 865 AA.
AC Q5YQD7;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=NFA_47520;
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX NCBI_TaxID=247156;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152;
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD59604.1; -; Genomic_DNA.
DR RefSeq; WP_011211288.1; NC_006361.1.
DR AlphaFoldDB; Q5YQD7; -.
DR SMR; Q5YQD7; -.
DR STRING; 247156.NFA_47520; -.
DR EnsemblBacteria; BAD59604; BAD59604; NFA_47520.
DR GeneID; 61135351; -.
DR KEGG; nfa:NFA_47520; -.
DR eggNOG; COG1060; Bacteria.
DR HOGENOM; CLU_010522_1_0_11; -.
DR OMA; HWVGHLN; -.
DR BioCyc; NFAR247156:NFA_RS23570-MON; -.
DR UniPathway; UPA00072; -.
DR Proteomes; UP000006820; 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; 2.
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..865
FT /note="FO synthase"
FT /id="PRO_0000147773"
FT DOMAIN 76..320
FT /note="Radical SAM core 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DOMAIN 544..785
FT /note="Radical SAM core 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..409
FT /note="CofG-like"
FT REGION 521..854
FT /note="CofH-like"
FT BINDING 90
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 94
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 97
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 558
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 562
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 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"
SQ SEQUENCE 865 AA; 93767 MW; BC64ED541BFF7553 CRC64;
MIEGVTELAT PNVPPAPPSP SAMRRALRRA RDGVSLNLDE AVVLLHARGD DLADLCRSAA
RVRDAGLESA GRPGTITYSR NVFIPLTRLC RDRCHYCTFV TVPGKLRAEG KGMFLEPDEV
LDIARRGAAL GCKEALFTLG DRPEDRWPEA AQWLDERGYD STLDYLRAVS ILVLEETGLL
PHLNPGVMSW AEIARLKPVA QSMGMMLETT ATRLFTEKGQ CHHGSPDKDP AVRLRAITDA
GRLSVPYTTG ILVGIGETLT ERAESIMAIR KQHKAFGHIQ EVIVQNFRAK DDTAMRDAPD
AGFDEFRATI AVTRLLLGPD VPVQAPPNLV SQQECLALIE AGIDDWGGVS PVTPDHVNPE
RPWPNLDTLR ELTEASGFTL VERTSAHPKY VRAGNPWIDP RIGAHVAALT DPVTGLAKAD
ALPVGLPWQE PDESWESAGR TDLNIAIDTE GRNTEARSDA ALGQDVVGAF GDWDTIREQV
RDLAVNAPER LDSDVLAALR AAERDPAGLS DDQYLALATA DGAELDAVAA LADQLRRDTV
GDDVTYVVNR NINFTNICYT GCRFCAFAQR KGDADAFTLS TEEVADRAWE AYVDGATEVC
MQGGIDPDLP VTGYADLVRA VKRRVPSMHV HAFSPMEIVN GASRGGESIA DWLTALKEAG
LDTIPGTAAE ILDDEVRWVL TKGKLPSSAW IEVITTAHRV GLRSSSTMMY GHVDNPSHWV
GHLRVLRGIQ DETGGFTEFV LLPFVHQSAP LYLAGAARPG PTIRDNRAAH ALARIMLHGR
IDNIQTSWVK LGIAGTRVML QGGANDLGGT LMEETISRMA GSQHGSAKTV AELAEIAEGI
GRPVRERTTV YGRVDRRPAP IVPVG
