FBIC_MYCBO
ID FBIC_MYCBO Reviewed; 856 AA.
AC Q7U0G9; A0A1R3XXK4; Q7B8A4; X2BH81;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=BQ2027_MB1206;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ROLE IN COENZYME F420 AND FO
RP BIOSYNTHESIS.
RC STRAIN=BCG;
RX PubMed=11948155; DOI=10.1128/jb.184.9.2420-2428.2002;
RA Choi K.-P., Kendrick N., Daniels L.;
RT "Demonstration that fbiC is required by Mycobacterium bovis BCG for
RT coenzyme F(420) and FO biosynthesis.";
RL J. Bacteriol. 184:2420-2428(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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:0000305|PubMed:11948155}.
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; AF479769; AAL91922.1; -; Genomic_DNA.
DR EMBL; LT708304; SIT99807.1; -; Genomic_DNA.
DR RefSeq; NP_854860.1; NC_002945.3.
DR RefSeq; WP_003406167.1; NC_002945.4.
DR AlphaFoldDB; Q7U0G9; -.
DR SMR; Q7U0G9; -.
DR EnsemblBacteria; SIT99807; SIT99807; BQ2027_MB1206.
DR GeneID; 45425145; -.
DR PATRIC; fig|233413.5.peg.1325; -.
DR OMA; HWVGHLN; -.
DR BioCyc; MetaCyc:MON-12180; -.
DR BRENDA; 2.5.1.147; 3494.
DR BRENDA; 4.3.1.32; 3494.
DR UniPathway; UPA00072; -.
DR Proteomes; UP000001419; 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; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..856
FT /note="FO synthase"
FT /id="PRO_0000147769"
FT DOMAIN 84..336
FT /note="Radical SAM core 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DOMAIN 544..785
FT /note="Radical SAM core 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT REGION 85..417
FT /note="CofG-like"
FT REGION 521..854
FT /note="CofH-like"
FT BINDING 98
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 102
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 105
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 558
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 562
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 565
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 856 AA; 92506 MW; 1D9E2FCAE82A7CD9 CRC64;
MPQPVGRKST ALPSPVVPPQ ANASALRRVL RRARDGVTLN VDEAAIAMTA RGDELADLCA
SAARVRDAGL VSAGRHGPSG RLAISYSRKV FIPVTRLCRD NCHYCTFVTV PGKLRAQGSS
TYMEPDEILD VARRGAEFGC KEALFTLGDR PEARWRQARE WLGERGYDST LSYVRAMAIR
VLEQTGLLPH LNPGVMSWSE MSRLKPVAPS MGMMLETTSR RLFETKGLAH YGSPDKDPAV
RLRVLTDAGR LSIPFTTGLL VGIGETLSER ADTLHAIRKS HKEFGHIQEV IVQNFRAKEH
TAMAAFPDAG IEDYLATVAV ARLVLGPGMR IQAPPNLVSG DECRALVGAG VDDWGGVSPL
TPDHVNPERP WPALDELAAV TAEAGYDMVQ RLTAQPKYVQ AGAAWIDPRV RGHVVALADP
ATGLARDVNP VGMPWQEPDD VASWGRVDLG AAIDTQGRNT AVRSDLASAF GDWESIREQV
HELAVRAPER IDTDVLAALR SAERAPAGCT DGEYLALATA DGPALEAVAA LADSLRRDVV
GDEVTFVVNR NINFTNICYT GCRFCAFAQR KGDADAYSLS VGEVADRAWE AHVAGATEVC
MQGGIDPELP VTGYADLVRA VKARVPSMHV HAFSPMEIAN GVTKSGLSIR EWLIGLREAG
LDTIPGTAAE ILDDEVRWVL TKGKLPTSLW IEIVTTAHEV GLRSSSTMMY GHVDSPRHWV
AHLNVLRDIQ DRTGGFTEFV PLPFVHQNSP LYLAGAARPG PSHRDNRAVH ALARIMLHGR
ISHIQTSWVK LGVRRTQVML EGGANDLGGT LMEETISRMA GSEHGSAKTV AELVAIAEGI
GRPARQRTTT YALLAA
