ID A0A3G8JVW8_9ACTN Unreviewed; 415 AA.
AC A0A3G8JVW8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase {ECO:0000256|ARBA:ARBA00012126};
DE EC=4.3.1.32 {ECO:0000256|ARBA:ARBA00012126};
GN Name=fbiC_2 {ECO:0000313|EMBL:AZG48742.1};
GN ORFNames=D7316_05363 {ECO:0000313|EMBL:AZG48742.1};
OS Gordonia insulae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=2420509 {ECO:0000313|EMBL:AZG48742.1, ECO:0000313|Proteomes:UP000271469};
RN [1] {ECO:0000313|EMBL:AZG48742.1, ECO:0000313|Proteomes:UP000271469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS17-SY073 {ECO:0000313|EMBL:AZG48742.1,
RC ECO:0000313|Proteomes:UP000271469};
RA Kim Y.S., Kim S.B.;
RT "Gordonia insulae sp. nov., isolated from an island soil.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
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DR EMBL; CP033972; AZG48742.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G8JVW8; -.
DR KEGG; gom:D7316_05363; -.
DR OrthoDB; 9802027at2; -.
DR UniPathway; UPA00072; -.
DR Proteomes; UP000271469; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
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 GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_01611; FO_synth_sub1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR019939; CofG_family.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR034405; F420.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR03550; F420_cofG; 1.
DR PANTHER; PTHR43076; FO SYNTHASE (COFH); 1.
DR PANTHER; PTHR43076:SF1; LIPOYL SYNTHASE 2; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00294; 7_8-didemethyl-8-hydroxy-5-dea; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
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:UP000271469};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000313|EMBL:AZG48742.1}.
FT DOMAIN 60..310
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 415 AA; 44583 MW; EC3C0B34726ECFE3 CRC64;
MTGTVSVAAA LAAARSGAPI DRAQATSLLA CSGDELIELQ EIAATLRDDG LAAVGRDRQI
TYSRKVFIPL TRLCRDRCHY CTFVTVPGKL AREGHGMYLD LDEVVDIARK GAELGCKEAL
FTLGDRPEAR WSQAGEWLAA RGYTSTLDYV RAAAVAVLED TGLLPHLNPG VMSAEEMRRL
RPVAPSMGMM LETTSRRLFT DKGQPHYGSP DKDPLVRLQV LHDAGAERIP FTTGILVGIG
ETLTERAESI LAMAEVQRAH GHIQEVIVQN FRAKPDTAMR GTPDAEMTEF LAAVAVARIV
LGPHMRVQAP PNLVSREECA ALVASGIDDW GGVSPLTPDH VNPERPWPNL DVLAEITAST
GHTLTERITA QPPYVLGGDE WIDPSLAHHV AALADPATGL AAAVKPQGRP WSAVA
//
