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Database: UniProt
Entry: L8P8B3_STRVR
LinkDB: L8P8B3_STRVR
Original site: L8P8B3_STRVR 
ID   L8P8B3_STRVR            Unreviewed;       474 AA.
AC   L8P8B3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Bifunctional F420 biosynthesis protein FbiB {ECO:0000256|HAMAP-Rule:MF_01259};
DE   Includes:
DE     RecName: Full=Coenzyme F420:L-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_01259};
DE              EC=6.3.2.31 {ECO:0000256|HAMAP-Rule:MF_01259};
DE              EC=6.3.2.34 {ECO:0000256|HAMAP-Rule:MF_01259};
DE     AltName: Full=Coenzyme F420-0:L-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_01259};
DE     AltName: Full=Coenzyme F420-1:gamma-L-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_01259};
DE   Includes:
DE     RecName: Full=Dehydro-coenzyme F420-0 reductase {ECO:0000256|HAMAP-Rule:MF_01259};
DE              EC=1.3.8.17 {ECO:0000256|HAMAP-Rule:MF_01259};
GN   Name=fbiB {ECO:0000256|HAMAP-Rule:MF_01259};
GN   ORFNames=STVIR_5268 {ECO:0000313|EMBL:ELS53836.1};
OS   Streptomyces viridochromogenes Tue57.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1160705 {ECO:0000313|EMBL:ELS53836.1, ECO:0000313|Proteomes:UP000011205};
RN   [1] {ECO:0000313|EMBL:ELS53836.1, ECO:0000313|Proteomes:UP000011205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tue57 {ECO:0000313|EMBL:ELS53836.1,
RC   ECO:0000313|Proteomes:UP000011205};
RX   PubMed=23788550;
RA   Gruning B.A., Erxleben A., Hahnlein A., Gunther S.;
RT   "Draft Genome Sequence of Streptomyces viridochromogenes Strain Tu57,
RT   Producer of Avilamycin.";
RL   Genome Announc. 1:E00384-13(2013).
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes the GTP-dependent
CC       successive addition of two or more 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:0000256|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:0000256|HAMAP-
CC         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:0000256|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:0000256|HAMAP-
CC         Rule:MF_01259};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01259};
CC       Note=Monovalent cation. The ion could be potassium. {ECO:0000256|HAMAP-
CC       Rule:MF_01259};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01259};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01259};
CC       Note=Binds 2 divalent metal cations per subunit. The ions could be
CC       magnesium and/or manganese. {ECO:0000256|HAMAP-Rule:MF_01259};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01259}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the CofE family.
CC       {ECO:0000256|HAMAP-Rule:MF_01259}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01259}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELS53836.1}.
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DR   EMBL; AMLP01000155; ELS53836.1; -; Genomic_DNA.
DR   AlphaFoldDB; L8P8B3; -.
DR   PATRIC; fig|1160705.3.peg.5210; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000011205; Unassembled WGS sequence.
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; 3.30.1330.100; CofE-like; 2.
DR   Gene3D; 3.40.109.10; NADH Oxidase; 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   NCBIfam; TIGR01916; F420_cofE; 1.
DR   NCBIfam; TIGR03553; F420_FbiB_CTERM; 1.
DR   PANTHER; PTHR47917; -; 1.
DR   PANTHER; PTHR47917:SF1; COENZYME F420:L-GLUTAMATE LIGASE; 1.
DR   Pfam; PF01996; F420_ligase; 1.
DR   Pfam; PF00881; Nitroreductase; 1.
DR   SUPFAM; SSF144010; CofE-like; 1.
DR   SUPFAM; SSF55469; FMN-dependent nitroreductase-like; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_01259};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01259};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01259};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01259};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01259};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW   Rule:MF_01259};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01259};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01259};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_01259}.
FT   DOMAIN          55..246
FT                   /note="Coenzyme F420:L-glutamate ligase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01996"
FT   DOMAIN          284..454
FT                   /note="Nitroreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00881"
FT   REGION          1..274
FT                   /note="Coenzyme F420:L-glutamate ligase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..474
FT                   /note="Dehydro-coenzyme F420-0 reductase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT   REGION          452..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..474
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         55..58
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT   BINDING         85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT   BINDING         90
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT   BINDING         136
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT   BINDING         139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT   BINDING         177
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT   BINDING         178
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT   BINDING         314
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT   BINDING         346
FT                   /ligand="coenzyme F420-(gamma-Glu)n"
FT                   /ligand_id="ChEBI:CHEBI:133980"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT   BINDING         425
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT   BINDING         462
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
SQ   SEQUENCE   474 AA;  48730 MW;  6F2D8BE6D3001774 CRC64;
     MSGEESTAAP GTSAGGAVAG AADGGGPDAV GRGGAGRAPA SGGAPGYRVW AVSGIPEVAA
     GDDLAKVIAA AEPGLADGDV LLVTSKIVSK AEGRVVAAGD RESAIDAETV RVVARRGTLR
     IVENRQGLVM AAAGVDASNT PAGTVLLLPE DPDASARAIR EGLREALGVS VGVVVTDTFG
     RPWRSGLTDV AIGAAGVRVL DDLRGGTDAY GNPLSATVVA TADELAAAGD LVKGKAAGLP
     VAVVRGLAHT VAEEHGEGAR ALVRGARDDM FRLGTSEAIR EAVTQRRTVR AFADEPVDPG
     AVRRAVAAAV TAPAPHHTTP WRFVLLESAE SRTRLLDAMR DAWIADLRRD GKSEESTAKR
     VRRGDVLRNA PYLVVPCLVM DGSHTYGDAR RDGAEREMFV VAAGAGVQNF LVALAGERLG
     SAWVSSTMFC RDVVRGVLGL PADWDPMGAV AVGHPAEEPR PRPERDAGAF IEVR
//
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