ID A0A0P0SE36_9PSEU Unreviewed; 862 AA.
AC A0A0P0SE36;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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:ALL82576.1};
GN ORFNames=AD017_17775 {ECO:0000313|EMBL:ALL82576.1};
OS Pseudonocardia sp. EC080619-01.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL82576.1, ECO:0000313|Proteomes:UP000066228};
RN [1] {ECO:0000313|EMBL:ALL82576.1, ECO:0000313|Proteomes:UP000066228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL82576.1,
RC ECO:0000313|Proteomes:UP000066228};
RX PubMed=26535611; DOI=10.1021/jacs.5b09794;
RA Van Arnam E.B., Sit C.S.;
RT "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense.";
RL J. Am. Chem. Soc. 137:14272-14274(2015).
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}.
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DR EMBL; CP012184; ALL82576.1; -; Genomic_DNA.
DR RefSeq; WP_010229368.1; NZ_CP012184.1.
DR AlphaFoldDB; A0A0P0SE36; -.
DR STRING; 1096856.AD017_17775; -.
DR KEGG; pecq:AD017_17775; -.
DR PATRIC; fig|1096856.3.peg.3730; -.
DR OrthoDB; 9802027at2; -.
DR UniPathway; UPA00072; -.
DR Proteomes; UP000066228; 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: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:UP000066228};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 73..320
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 532..768
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 829..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 93275 MW; 228D8D1C87F10183 CRC64;
MADTPAAPVP AEAAPSDSAL RRALRRVRDG STLDVTEAAV LLAARGEHLD ELLSHAGRVR
DAGLVEEGRP GVVTYSRNVF IPLTRLCRDR CHYCTFATVP HRLDSMFLER DEVVEIARQG
AAQGCKEALF TLGDRPEERW PQAREWLEAR GYDSTLDYVR ACAIAVLEET GLLPHLNPGV
MSWEEITRLK PVAASMGMML ETTSQRLFEK GGPHFGSPDK EPAVRVRALA DAGRVGVPFT
TGILIGIGEN RTERAESLFA IRSAARQHGH VQEVIVQNFR AKPDTAMAND PDADLDDLAA
TIAVSRLVLG PKVRLQAPPN LVGDEQALML RAGIDDWGGV SPVTVDHVSP EMPWPAVDEL
ARVTAEEGFE LRERLTAYPK YVRAGSPWID TRLHGHVAAL ATPDGLADPG AVVQGLPWQE
PDGGFESTGR TDLHTAVDTE GRTDDRRSDF GSVYGDWDEV AAELESQRAR APERLAGDVK
AGLELAASDP AALLDPANEA AAMAVLTGEG PALRELTRLA DDVRRQVNGD DVTYVVNRNI
NFSNVCYVGC RFCAFAQRER DADAFRLSLD EIAQRAAEAA RDGATEVCVQ GGIDPQLPVS
FYADLVRAVH EAVPGMHVHA FSPMEIVSAA AKAGVSIREW LSELKAAGLG SIPGTAAEIL
DDEVRWVLTK GKLPASQWIE VVSTAHELGI PSSSTMMYGH VDEPRHWLGH LRTLASVQDR
TGGFTEFVPL PFVHHNAPIY LAGIARPGPT ERDNRAVHAF ARLALHGRID HVQVSWVKLG
DELAGQVLNG GADDMGGTLM EETISRMAGS ENGSERSVEE LTEIAHAAGR PVRQRTTTYR
GEPSVLTPAR PSGPRMLPLA PA
//
