ID A0A0F5W2I6_9ACTN Unreviewed; 433 AA.
AC A0A0F5W2I6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=TN53_06835 {ECO:0000313|EMBL:KKD08553.1};
OS Streptomyces sp. WM6386.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415558 {ECO:0000313|EMBL:KKD08553.1, ECO:0000313|Proteomes:UP000033641};
RN [1] {ECO:0000313|EMBL:KKD08553.1, ECO:0000313|Proteomes:UP000033641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM6386 {ECO:0000313|EMBL:KKD08553.1,
RC ECO:0000313|Proteomes:UP000033641};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KKD08553.1}.
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DR EMBL; JXTE01000008; KKD08553.1; -; Genomic_DNA.
DR RefSeq; WP_046257480.1; NZ_JXTE01000008.1.
DR AlphaFoldDB; A0A0F5W2I6; -.
DR PATRIC; fig|1415558.3.peg.8375; -.
DR OrthoDB; 9788295at2; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000033641; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000033641}.
FT DOMAIN 14..205
FT /note="Coenzyme F420:L-glutamate ligase-like"
FT /evidence="ECO:0000259|Pfam:PF01996"
FT DOMAIN 243..413
FT /note="Nitroreductase"
FT /evidence="ECO:0000259|Pfam:PF00881"
FT REGION 1..233
FT /note="Coenzyme F420:L-glutamate ligase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT REGION 234..433
FT /note="Dehydro-coenzyme F420-0 reductase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT REGION 410..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 44
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 49
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 95
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 98
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 137
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 273
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 305
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 384
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 421
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
SQ SEQUENCE 433 AA; 45843 MW; 02B99CDFB8CE3DD7 CRC64;
MTTDGFRAWA VPGLPEIAPG DDLAKLIAAA EPGLADGDVL LVTSKIVSKA EGRVVEAADR
EAAIDAETVR VVARRGALRI VENRQGLIMA AAGVDASNTP AGTVLLLPED PDAAARAIRE
GLRDLLGVQV GVVVTDTFGR PWRAGLTDVA IGAAGVRVLD DLRGGTDAYG NPLSATVVAT
ADELAAAGDL VKGKAAGLPV AVVRGLAHVV AEEHGEGAGA MVRGARDDMF RLGTSEAIRQ
AVTQRRTVRA FTDEPVDPGA VRRAVAAAVT APAPHHTTPW RFVLLESAES RTRLLDAMRD
AWIGDLRRDR KSEESIAKRV KRGDVLRNAP YLVVPCLVMD GSHDYGDPRR DGAEREMFVV
ATGAGVQNFL VALAGERLGS AWVSSTMFCR DVVREVLGLP RDWDPMGAVA VGHPAEEPRP
RPDRDAGMFI EVR
//
