FBIB_MYCBO
ID FBIB_MYCBO Reviewed; 448 AA.
AC Q7TWV3; A0A1R3Y3L5; X2BMN4;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Bifunctional F420 biosynthesis protein FbiB {ECO:0000255|HAMAP-Rule:MF_01259};
DE Includes:
DE RecName: Full=Coenzyme F420:L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_01259};
DE EC=6.3.2.31 {ECO:0000255|HAMAP-Rule:MF_01259};
DE EC=6.3.2.34 {ECO:0000255|HAMAP-Rule:MF_01259};
DE AltName: Full=Coenzyme F420-0:L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_01259};
DE AltName: Full=Coenzyme F420-1:gamma-L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_01259};
DE Includes:
DE RecName: Full=Dehydro-coenzyme F420-0 reductase {ECO:0000255|HAMAP-Rule:MF_01259};
DE EC=1.3.8.17 {ECO:0000255|HAMAP-Rule:MF_01259};
GN Name=fbiB {ECO:0000255|HAMAP-Rule:MF_01259};
GN OrderedLocusNames=BQ2027_MB3290;
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 [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 [2]
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).
RN [3]
RP ROLE IN COENZYME F420 BIOSYNTHESIS, AND DISRUPTION PHENOTYPE.
RC STRAIN=BCG;
RX PubMed=11717263; DOI=10.1128/jb.183.24.7058-7066.2001;
RA Choi K.-P., Bair T.B., Bae Y.-M., Daniels L.;
RT "Use of transposon Tn5367 mutagenesis and a nitroimidazopyran-based
RT selection system to demonstrate a requirement for fbiA and fbiB in coenzyme
RT F(420) biosynthesis by Mycobacterium bovis BCG.";
RL J. Bacteriol. 183:7058-7066(2001).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the GTP-dependent
CC successive addition of multiple gamma-linked L-glutamates to the L-
CC lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin
CC (F420-0) to form polyglutamated F420 derivatives, and the FMNH2-
CC dependent reduction of dehydro-F420-0 to form F420-0.
CC {ECO:0000255|HAMAP-Rule:MF_01259}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) +
CC oxidized coenzyme F420-1 + phosphate; Xref=Rhea:RHEA:30555,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189, ChEBI:CHEBI:59907,
CC ChEBI:CHEBI:59920; EC=6.3.2.31; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01259};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + L-glutamate + oxidized coenzyme F420-1 = GDP + H(+) +
CC oxidized coenzyme F420-2 + phosphate; Xref=Rhea:RHEA:30523,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57922, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:59920; EC=6.3.2.34; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01259};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + L-glutamate + oxidized coenzyme F420-(gamma-L-Glu)(n) =
CC GDP + H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n+1) + phosphate;
CC Xref=Rhea:RHEA:51236, Rhea:RHEA-COMP:12939, Rhea:RHEA-COMP:12940,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189, ChEBI:CHEBI:133980;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01259};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=FMN + H(+) + oxidized coenzyme F420-0 = dehydro coenzyme F420-
CC 0 + FMNH2; Xref=Rhea:RHEA:60360, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:59907,
CC ChEBI:CHEBI:143705; EC=1.3.8.17; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01259};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01259};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01259};
CC Note=Binds 2 divalent metal cations per subunit. The ions could be
CC magnesium and/or manganese. {ECO:0000255|HAMAP-Rule:MF_01259};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01259};
CC Note=Monovalent cation. The ion could be potassium. {ECO:0000255|HAMAP-
CC Rule:MF_01259};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01259, ECO:0000269|PubMed:11717263}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene cannot make F420-5,6 as
CC the wild-type, but are able to make the biosynthesis of the
CC intermediate FO. {ECO:0000269|PubMed:11717263}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CofE family.
CC {ECO:0000255|HAMAP-Rule:MF_01259, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT708304; SIU01919.1; -; Genomic_DNA.
DR RefSeq; NP_856935.1; NC_002945.3.
DR RefSeq; WP_003900663.1; NC_002945.4.
DR AlphaFoldDB; Q7TWV3; -.
DR SMR; Q7TWV3; -.
DR EnsemblBacteria; SIU01919; SIU01919; BQ2027_MB3290.
DR GeneID; 45427256; -.
DR PATRIC; fig|233413.5.peg.3617; -.
DR OMA; VGSCWIG; -.
DR BRENDA; 1.3.8.17; 3494.
DR BRENDA; 6.3.2.31; 3494.
DR BRENDA; 6.3.2.34; 3494.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0052618; F:coenzyme F420-0:L-glutamate ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0052619; F:coenzyme F420-1:gamma-L-glutamate ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052890; F:oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0052645; P:F420-0 metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.109.10; -; 1.
DR HAMAP; MF_01259; F420_ligase_FbiB; 1.
DR InterPro; IPR008225; F420-0_g-glutamyl_ligase.
DR InterPro; IPR002847; F420-0_gamma-glut_ligase-dom.
DR InterPro; IPR019943; F420_FbiB_C.
DR InterPro; IPR023661; FbiB.
DR InterPro; IPR029479; Nitroreductase.
DR InterPro; IPR000415; Nitroreductase-like.
DR Pfam; PF01996; F420_ligase; 1.
DR Pfam; PF00881; Nitroreductase; 1.
DR SUPFAM; SSF55469; SSF55469; 1.
DR TIGRFAMs; TIGR01916; F420_cofE; 1.
DR TIGRFAMs; TIGR03553; F420_FbiB_CTERM; 1.
PE 3: Inferred from homology;
KW GTP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW Multifunctional enzyme; Nucleotide-binding; Oxidoreductase; Potassium.
FT CHAIN 1..448
FT /note="Bifunctional F420 biosynthesis protein FbiB"
FT /id="PRO_0000145777"
FT REGION 1..244
FT /note="Coenzyme F420:L-glutamate ligase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
FT REGION 245..448
FT /note="Dehydro-coenzyme F420-0 reductase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
FT BINDING 20..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
FT BINDING 50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
FT BINDING 55
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
FT BINDING 109
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
FT BINDING 112
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
FT BINDING 150
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
FT BINDING 151
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
FT BINDING 260..264
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
FT BINDING 288
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
FT BINDING 320
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
FT BINDING 399
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
FT BINDING 436
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
SQ SEQUENCE 448 AA; 47578 MW; 8C6DB75DE6E86851 CRC64;
MTGPEHGSAS TIEILPVIGL PEFRPGDDLS AAVAAAAPWL RDGDVVVVTS KVVSKCEGRL
VPAPEDPEQR DRLRRKLIED EAVRVLARKD RTLITENRLG LVQAAAGVDG SNVGRSELAL
LPVDPDASAA TLRAGLRERL GVTVAVVITD TMGRAWRNGQ TDAAVGAAGL AVLRNYAGVR
DPYGNELVVT EVAVADEIAA AADLVKGKLT ATPVAVVRGF GVSDDGSTAR QLLRPGANDL
FWLGTAEALE LGRQQAQLLR RSVRRFSTDP VPGDLVEAAV AEALTAPAPH HTRPTRFVWL
QTPAIRARLL DRMKDKWRSD LTSDGLPADA IERRVARGQI LYDAPEVVIP MLVPDGAHSY
PDAARTDAEH TMFTVAVGAA VQALLVALAV RGLGSCWIGS TIFAADLVRD ELDLPVDWEP
LGAIAIGYAD EPSGLRDPVP AADLLILK
