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Database: UniProt
Entry: A0A0E8VJ82_MYCTX
LinkDB: A0A0E8VJ82_MYCTX
Original site: A0A0E8VJ82_MYCTX 
ID   A0A0E8VJ82_MYCTX        Unreviewed;       809 AA.
AC   A0A0E8VJ82;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
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:SGI57086.1};
GN   Synonyms=mqnE {ECO:0000313|EMBL:OMH59090.1};
GN   ORFNames=A4S10_01253 {ECO:0000313|EMBL:OMH59090.1}, ERS053720_03572
GN   {ECO:0000313|EMBL:CFH95325.1}, SAMEA2683035_03884
GN   {ECO:0000313|EMBL:SGI57086.1};
OS   Mycobacterium tuberculosis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=1773 {ECO:0000313|EMBL:SGI57086.1, ECO:0000313|Proteomes:UP000182946};
RN   [1] {ECO:0000313|EMBL:CFH95325.1, ECO:0000313|Proteomes:UP000046674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0351H {ECO:0000313|EMBL:CFH95325.1,
RC   ECO:0000313|Proteomes:UP000046674};
RG   Pathogen Informatics;
RA   Murphy D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OMH59090.1, ECO:0000313|Proteomes:UP000189452}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6548 {ECO:0000313|EMBL:OMH59090.1,
RC   ECO:0000313|Proteomes:UP000189452};
RA   Bigi M., Bigi F., Soria M.A.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SGI57086.1, ECO:0000313|Proteomes:UP000182946}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2926STDY5723788 {ECO:0000313|EMBL:SGI57086.1,
RC   ECO:0000313|Proteomes:UP000182946};
RG   Pathogen Informatics;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:OMH59090.1, ECO:0000313|Proteomes:UP000189452}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6548 {ECO:0000313|EMBL:OMH59090.1,
RC   ECO:0000313|Proteomes:UP000189452};
RA   Bigi M.M., Lopez B., Blanco F.C., Sasiain M.C., De La Barrera S.,
RA   Ritacco V., Bigi F., Soria M.A.;
RT   "Protein polymorphisms may explain contrasting epidemiological fitness of
RT   two variants of a multidrug-resistant Mycobacterium tuberculosis strain.";
RL   Submitted (FEB-2017) 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; CFSW01000028; CFH95325.1; -; Genomic_DNA.
DR   EMBL; LWDQ01000001; OMH59090.1; -; Genomic_DNA.
DR   EMBL; FPTZ01000042; SGI57086.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E8VJ82; -.
DR   PATRIC; fig|1773.211.peg.88; -.
DR   UniPathway; UPA00072; -.
DR   Proteomes; UP000046674; Unassembled WGS sequence.
DR   Proteomes; UP000182946; Unassembled WGS sequence.
DR   Proteomes; UP000189452; 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; 2.
DR   SFLD; SFLDF00343; aminofutalosine_synthase_(mqnE; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 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   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000313|EMBL:OMH59090.1}.
FT   DOMAIN          37..289
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   DOMAIN          497..738
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   809 AA;  87577 MW;  D353A1424F8BEBB1 CRC64;
     MTARGDELAD LCASAARVRD AGLVSAGRHG PSGRLAISYS RKVFIPVTRL CRDNCHYCTF
     VTVPGKLRAQ GSSTYMEPDE ILDVARRGAE FGCKEALFTL GDRPEARWRQ AREWLGERGY
     DSTLSYVRAM AIRVLEQTGL LPHLNPGVMS WSEMSRLKPV APSMGMMLET TSRRLFETKG
     LAHYGSPDKD PAVRLRVLTD AGRLSIPFTT GLLVGIGETL SERADTLHAI RKSHKEFGHI
     QEVIVQNFRA KEHTAMAAFP DAGIEDYLAT VAVARLVLGP GMRIQAPPNL VSGDECRALV
     GAGVDDWGGV SPLTPDHVNP ERPWPALDEL AAVTAEAGYD MVQRLTAQPK YVQAGAAWID
     PRVRGHVVAL ADPATGLARD VNPVGMPWQE PDDVASWGRV DLGAAIDTQG RNTAVRSDLA
     SAFGDWESIR EQVHELAVRA PERIDTDVLA ALRSAERAPA GCTDGEYLAL ATADGPALEA
     VAALADSLRR DVVGDEVTFV VNRNINFTNI CYTGCRFCAF AQRKGDADAY SLSVGEVADR
     AWEAHVAGAT EVCMQGGIDP ELPVTGYADL VRAVKARVPS MHVHAFSPME IANGVTKSGL
     SIREWLIGLR EAGLDTIPGT AAEILDDEVR WVLTKGKLPT SLWIEIVTTA HEVGLRSSST
     MMYGHVDSPR HWVAHLNVLR DIQDRTGGFT EFVPLPFVHQ NSPLYLAGAA RPGPSHRDNR
     AVHALARIML HGRISHIQTS WVKLGVRRTQ VMLEGGANDL GGTLMEETIS RMAGSEHGSA
     KTVAELVAIA EGIGRPARQR TTTYALLAA
//
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