FBIC_STRAW
ID FBIC_STRAW Reviewed; 861 AA.
AC Q82GV2;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=SAV_3794;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
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; BA000030; BAC71506.1; -; Genomic_DNA.
DR RefSeq; WP_010985225.1; NZ_JZJK01000090.1.
DR AlphaFoldDB; Q82GV2; -.
DR SMR; Q82GV2; -.
DR STRING; 227882.SAV_3794; -.
DR EnsemblBacteria; BAC71506; BAC71506; SAVERM_3794.
DR KEGG; sma:SAVERM_3794; -.
DR eggNOG; COG1060; Bacteria.
DR HOGENOM; CLU_010522_1_0_11; -.
DR OMA; HWVGHLN; -.
DR OrthoDB; 419725at2; -.
DR UniPathway; UPA00072; -.
DR Proteomes; UP000000428; 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..861
FT /note="FO synthase"
FT /id="PRO_0000147774"
FT DOMAIN 69..319
FT /note="Radical SAM core 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DOMAIN 528..763
FT /note="Radical SAM core 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT REGION 70..401
FT /note="CofG-like"
FT REGION 505..838
FT /note="CofH-like"
FT BINDING 83
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 87
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 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 542
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 546
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 549
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 861 AA; 93933 MW; D7923745FD5610F0 CRC64;
MTTSATSGTG PTANSMRRAL KRARDGVALD VTEAAVLLQA RGEDLDDLTA SAARVRDAGL
EAAGRAGVIT YSKSVFIPLT RLCRDKCHYC TFVTVPGKLR RAGHGMFMSP DEVLDIARKG
AALGCKEALI TLGDKPEDRW PEAREWLDAH GYDDTIAYVR AISIRILEET GLLPHLNPGV
MSWTDFQRLK PVAPSMGMML ETTATRLWSE PGGPHHGSPD KEPAVRLRVL EDAGRSSVPF
TSGILIGIGE TYEERAESLF ALRKISRAYH GIQELIIQNF RAKPDTAMRG MPDAELDELI
ATVAVARHIM GPRACLQAPP NLVDSEYGRL IGAGIDDWGG VSPLTIDHVN PERPWPQIDL
LREQSAQAGF ELRERLCVYP EFVQRGEPWL DPRLLPHVRA LADPASGLAH ADATVEGHPW
QEPEEAFVAQ GRTDLHHSID TEGRTGDRRD DFDVVYGDWE ALREAAAPGM VPERIDTDVR
QALATAANDP TRLTDAEALA LLHADGPALD ALTRIADDVR KAAVGDDVTY IVTRNINFTN
VCYTGCRFCA FAQRRTDADA YTLSLEQVAD RAQQAWDVGA VEVCMQGGIH PDLPGTAYFD
IAKAVKERVP GMHVHAFSPM EVVNGATRTG LSIREWLTAA KEAGLDSIPG TAAEILDDEV
RWVLTKGKLP TATWIEVITT AHELGIRSSS TMMYGHVDQP RHWLGHFRTL ARIQQQTGGF
TEFVTLPFIH TNAPVYLAGI ARPGPTTRDN RAVMAMARLL LHPHIPNIQT SWVKLGTEGA
AEMLRSGAND LGGTLMEETI SRMAGSSYGS YKSVKDLIAV AEAAGRPAKP RTTLYGEVPQ
ERQRAAAASD GHLPELLPVL D
