ID A0A0J6XU35_9ACTN Unreviewed; 854 AA.
AC A0A0J6XU35;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=FO synthase {ECO:0000256|ARBA:ARBA00022220};
DE EC=2.5.1.147 {ECO:0000256|ARBA:ARBA00012289};
DE EC=4.3.1.32 {ECO:0000256|ARBA:ARBA00012126};
GN Name=fbiC {ECO:0000313|EMBL:KMO99630.1};
GN ORFNames=ACS04_01210 {ECO:0000313|EMBL:KMO99630.1};
OS Streptomyces roseus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=66430 {ECO:0000313|EMBL:KMO99630.1, ECO:0000313|Proteomes:UP000035932};
RN [1] {ECO:0000313|EMBL:KMO99630.1, ECO:0000313|Proteomes:UP000035932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31245 {ECO:0000313|EMBL:KMO99630.1,
RC ECO:0000313|Proteomes:UP000035932};
RA Cruz-Morales P., Martinez-Guerrero C., Morales-Escalante M.A.,
RA Yanez-Guerra L.A., Kopp J.F., Feldmann J., Ramos-Aboites H.E.,
RA Barona-Gomez F.;
RT "Recapitulation of the evolution of biosynthetic gene clusters reveals
RT hidden chemical diversity on bacterial genomes.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00003692}.
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 Evidence={ECO:0000256|ARBA:ARBA00000328};
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 Evidence={ECO:0000256|ARBA:ARBA00000403};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F0 biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004712}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the radical SAM
CC superfamily. CofH family. {ECO:0000256|ARBA:ARBA00010051}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the radical SAM
CC superfamily. CofG family. {ECO:0000256|ARBA:ARBA00010826}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMO99630.1}.
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DR EMBL; LFML01000006; KMO99630.1; -; Genomic_DNA.
DR RefSeq; WP_048474546.1; NZ_LFML01000006.1.
DR AlphaFoldDB; A0A0J6XU35; -.
DR STRING; 66430.ACS04_01210; -.
DR PATRIC; fig|66430.4.peg.5537; -.
DR OrthoDB; 9802027at2; -.
DR UniPathway; UPA00072; -.
DR Proteomes; UP000035932; Unassembled WGS sequence.
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:0044689; F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01335; Radical_SAM; 2.
DR Gene3D; 3.20.20.70; Aldolase class I; 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/MiaA/NifB-like_rSAM.
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; TIGR03550; F420_cofG; 1.
DR NCBIfam; TIGR03551; F420_cofH; 1.
DR PANTHER; PTHR43076; FO SYNTHASE (COFH); 1.
DR PANTHER; PTHR43076:SF1; LIPOYL SYNTHASE 2; 1.
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; SFLDG01388; 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; 2.
DR SUPFAM; SSF102114; Radical SAM enzymes; 2.
DR PROSITE; PS51918; RADICAL_SAM; 2.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000035932};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 62..312
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 521..764
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 854 AA; 93185 MW; 0C066DC8596B77F6 CRC64;
MTTPTENAMR RALRRARDGV ALDATEAAVL LQARGEDLED LAASAARVRD AGLAAAGRPG
VITYSKSVFI PLTRLCRDKC HYCTFATVPG KLRRAGHGMF MSPDEVLDIA RRGAALGCKE
ALITLGDKPE DRWPEAREWL EAAGYSDTIS YVRAISILIL EETGLLPHLN PGVMSWADFQ
RLKPVAPSMG MMLETTATRL WSEPGGPHHG SPDKEPAVRL RVLEDAGRSS VPFTSGLLIG
IGETYEERAE SLFALRRVSR SYHGVQELII QNFRAKPDTA MRGMPDAELD DLVATVAVAR
HIMGPSGCLQ APPNLVDGEY ARLIRAGIDD WGGVSPLTPD HVNPERPWPQ IDVLAEQSAA
AGFELRERLC VYPEFVQRGE PWLDPRLLPH VRALADPQTG LANPEAEVVG RPWQEPDEGF
GSYGRTDLHA TIDTEGRTGD RREDFDDVYG DWEALREAAA PGMVPERIDT DVRAALAQAA
DDPTKLTDDQ ALALLHADGP ALDALCRIAD DLRKSVVGDE VTYIVTRNIN FTNVCYTGCR
FCAFAQRRTD ADAYTLSLDQ VADRAAQAWD VGAVEVCMQG GIHPDLPGTA YFDIARAVKK
RVPGMHVHAF SPMEVVNGAT RTGMSVREWL TAAKEAGLDS IPGTAAEILD DEVRWVLTKG
KLPTADWIDV ITTAHELGIR SSSTMMYGHV DQPRHWLGHF RTLARIQQRT GGFTEFVTLP
FIHTNAPVYL AGIARPGPTV RDNRAVTAMA RILLHPHITN IQTSWVKLGA QGAAEMLRSG
ANDLGGTLME ETISRMAGSS YGSYKSVRDL IAVAEAAGRP ARARTTLYGE VPQERQQAAR
ASDGHLPELL PVLD
//
