FBIB_MYCTU
ID FBIB_MYCTU Reviewed; 448 AA.
AC P9WP79; L0TDM4; P96867; Q7D5T5;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 45.
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, ECO:0000269|PubMed:26861878};
DE EC=6.3.2.34 {ECO:0000255|HAMAP-Rule:MF_01259, ECO:0000269|PubMed:26861878};
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:0000305|PubMed:30952857};
DE EC=1.3.8.17 {ECO:0000269|PubMed:30952857};
GN Name=fbiB {ECO:0000255|HAMAP-Rule:MF_01259}; OrderedLocusNames=Rv3262;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP CRYSTALLIZATION OF 245-448.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22102046; DOI=10.1107/s1744309111028958;
RA Rehan A.M., Bashiri G., Paterson N.G., Baker E.N., Squire C.J.;
RT "Cloning, expression, purification, crystallization and preliminary X-ray
RT studies of the C-terminal domain of Rv3262 (FbiB) from Mycobacterium
RT tuberculosis.";
RL Acta Crystallogr. F 67:1274-1277(2011).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP FUNCTION OF C-TERMINAL DOMAIN, AND CATALYTIC ACTIVITY OF C-TERMINAL DOMAIN.
RX PubMed=30952857; DOI=10.1038/s41467-019-09534-x;
RA Bashiri G., Antoney J., Jirgis E.N.M., Shah M.V., Ney B., Copp J.,
RA Stuteley S.M., Sreebhavan S., Palmer B., Middleditch M., Tokuriki N.,
RA Greening C., Scott C., Baker E.N., Jackson C.J.;
RT "A revised biosynthetic pathway for the cofactor F420 in prokaryotes.";
RL Nat. Commun. 10:1558-1558(2019).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 245-448 OF APOENZYME AND IN
RP COMPLEXES WITH FMN AND COENZYME GAMMA-F420-2, FUNCTION, CATALYTIC ACTIVITY
RP OF N-TERMINAL DOMAIN, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=26861878; DOI=10.1074/jbc.m115.689026;
RA Bashiri G., Rehan A.M., Sreebhavan S., Baker H.M., Baker E.N., Squire C.J.;
RT "Elongation of the Poly-gamma-glutamate Tail of F420 Requires Both Domains
RT of the F420:gamma-Glutamyl Ligase (FbiB) of Mycobacterium tuberculosis.";
RL J. Biol. Chem. 291:6882-6894(2016).
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, ECO:0000269|PubMed:26861878,
CC ECO:0000269|PubMed:30952857}.
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, ECO:0000269|PubMed:26861878};
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, ECO:0000269|PubMed:26861878};
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 ECO:0000269|PubMed:26861878};
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;
CC Evidence={ECO:0000269|PubMed:30952857};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:26861878};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01259}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CofE family.
CC {ECO:0000255|HAMAP-Rule:MF_01259}.
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DR EMBL; AL123456; CCP46081.1; -; Genomic_DNA.
DR PIR; G70977; G70977.
DR RefSeq; NP_217779.1; NC_000962.3.
DR RefSeq; WP_003900663.1; NZ_NVQJ01000003.1.
DR PDB; 4XOM; X-ray; 1.90 A; A/B/C/D=245-448.
DR PDB; 4XOO; X-ray; 2.10 A; A/B/C/D=245-448.
DR PDB; 4XOQ; X-ray; 2.05 A; A/B/C/D=245-448.
DR PDBsum; 4XOM; -.
DR PDBsum; 4XOO; -.
DR PDBsum; 4XOQ; -.
DR AlphaFoldDB; P9WP79; -.
DR SMR; P9WP79; -.
DR STRING; 83332.Rv3262; -.
DR PaxDb; P9WP79; -.
DR DNASU; 888693; -.
DR GeneID; 45427256; -.
DR GeneID; 888693; -.
DR KEGG; mtu:Rv3262; -.
DR TubercuList; Rv3262; -.
DR eggNOG; COG0778; Bacteria.
DR eggNOG; COG1478; Bacteria.
DR OMA; VGSCWIG; -.
DR PhylomeDB; P9WP79; -.
DR BioCyc; MetaCyc:G185E-7536-MON; -.
DR BRENDA; 1.3.8.17; 3445.
DR BRENDA; 6.3.2.31; 3445.
DR BRENDA; 6.3.2.34; 3445.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0052618; F:coenzyme F420-0:L-glutamate ligase activity; IBA:GO_Central.
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:2001121; P:coenzyme gamma-F420-2 biosynthetic process; IMP:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW Multifunctional enzyme; Nucleotide-binding; Oxidoreductase; Potassium;
KW Reference proteome.
FT CHAIN 1..448
FT /note="Bifunctional F420 biosynthesis protein FbiB"
FT /id="PRO_0000145780"
FT REGION 1..244
FT /note="Coenzyme F420:L-glutamate ligase"
FT REGION 245..448
FT /note="Dehydro-coenzyme F420-0 reductase"
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:0000269|PubMed:26861878,
FT ECO:0007744|PDB:4XOO"
FT BINDING 288
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:26861878,
FT ECO:0007744|PDB:4XOO"
FT BINDING 320
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000269|PubMed:26861878,
FT ECO:0007744|PDB:4XOQ"
FT BINDING 399
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:26861878,
FT ECO:0007744|PDB:4XOO"
FT BINDING 436
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:26861878,
FT ECO:0007744|PDB:4XOO"
FT HELIX 245..253
FT /evidence="ECO:0007829|PDB:4XOM"
FT HELIX 254..258
FT /evidence="ECO:0007829|PDB:4XOM"
FT HELIX 273..283
FT /evidence="ECO:0007829|PDB:4XOM"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:4XOM"
FT HELIX 303..323
FT /evidence="ECO:0007829|PDB:4XOM"
FT HELIX 328..335
FT /evidence="ECO:0007829|PDB:4XOM"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:4XOM"
FT HELIX 339..343
FT /evidence="ECO:0007829|PDB:4XOM"
FT STRAND 345..352
FT /evidence="ECO:0007829|PDB:4XOM"
FT HELIX 363..389
FT /evidence="ECO:0007829|PDB:4XOM"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:4XOM"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:4XOM"
FT HELIX 400..404
FT /evidence="ECO:0007829|PDB:4XOM"
FT HELIX 405..412
FT /evidence="ECO:0007829|PDB:4XOM"
FT STRAND 423..427
FT /evidence="ECO:0007829|PDB:4XOM"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:4XOM"
FT HELIX 442..444
FT /evidence="ECO:0007829|PDB:4XOM"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:4XOM"
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
