ID F8JG56_HYPSM Unreviewed; 797 AA.
AC F8JG56;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
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:CCB66757.1};
GN OrderedLocusNames=HYPMC_3547 {ECO:0000313|EMBL:CCB66757.1};
OS Hyphomicrobium sp. (strain MC1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=717785 {ECO:0000313|EMBL:CCB66757.1, ECO:0000313|Proteomes:UP000000494};
RN [1] {ECO:0000313|Proteomes:UP000000494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC1 {ECO:0000313|Proteomes:UP000000494};
RA Genoscope.;
RT "The complete genome of Hyphomicrobium sp. MC1.";
RL Submitted (MAY-2011) 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}.
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DR EMBL; FQ859181; CCB66757.1; -; Genomic_DNA.
DR RefSeq; WP_013949152.1; NC_015717.1.
DR AlphaFoldDB; F8JG56; -.
DR STRING; 717785.HYPMC_3547; -.
DR KEGG; hmc:HYPMC_3547; -.
DR eggNOG; COG1060; Bacteria.
DR HOGENOM; CLU_010522_0_0_5; -.
DR UniPathway; UPA00072; -.
DR Proteomes; UP000000494; 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; SFLDF00294; 7_8-didemethyl-8-hydroxy-5-dea; 1.
DR SFLD; SFLDG01388; 7_8-didemethyl-8-hydroxy-5-dea; 2.
DR SFLD; SFLDF00343; aminofutalosine_synthase_(mqnE; 1.
DR SFLD; SFLDG01064; F420__menaquinone_cofactor_bio; 1.
DR SMART; SM00729; Elp3; 1.
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:UP000000494};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000313|EMBL:CCB66757.1}.
FT DOMAIN 49..296
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 464..703
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 797 AA; 88275 MW; E7C804CC664423B5 CRC64;
MTGVSDILSR KSGSRLSRDE AMALVDLDDI APLLDAAARR RDAAHGDVVS YSRKVFIPLT
QLCRDVCHYC TFAHPPRKGE RAYLTRDEVL SIAMSGKKAG CKEALFTLGD KPELRYEFAR
DELRALGHDT TLSYVAEMAS VVLKETGLLP HINPGLMSDD DLLSLRSVAA SQGIMLESAS
ERLCEKGQVH YGSPDKAPAA RLDTIRRAGV HGIAFTSGIL IGIGETREER IDALVALRDL
NDQYGHIQEI IVQNFRPKPG TRMADVAAPT LDDHLWTIAI ARLLFEPEMN IQAPPNLSAG
DLPALVSAGI NDWGGVSPVT PDFVNPEAPW PHVRVLEQET SAVGKALRER VAIYPAFARQ
PSKWVDRTVL KPLFVMTDAD GWPRTDTWCV GRLEEPPAHD VKLVRARKSH QASDRIRAVL
DKVSDGRCLG EDDIVSLFRA QSDDFSAVCR AADELRRRTN GDVVSYVITR NINYTNICYF
KCQFCAFSKG KLSENLRGKP YDLGLDEIAH RAFEAWDRGA TEVCMQGGIH PSYTGQRYLD
ICNAVKTRVP QMHLHAFSPL EVAQGAKTLG ITVRSFLGQL KAAGLGTLPG TAAEILDDEV
RQQLCPDKLD SAEWLDVMRT AHLSGFKSTA TIMFGHIDRY EHWARHLLRI RNLQIETGGF
TEFVPLPFVH MEAPMYLKGR ARPGPTFREA ILMHAVSRLV LHPHITNIQA SWVKLGADGV
RLCLDAGVND LGGTLMDESI SRSAGASHGQ EMTPERMEEI IRTSGRQPRR RTTLYEMAST
ATREIRGVNA EEQQLSL
//
