ID A1UCJ4_MYCSK Unreviewed; 455 AA.
AC A1UCJ4;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 104.
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 OrderedLocusNames=Mkms_1340 {ECO:0000313|EMBL:ABL90552.1};
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL90552.1};
RN [1] {ECO:0000313|EMBL:ABL90552.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS {ECO:0000313|EMBL:ABL90552.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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: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-(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:0000256|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: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}.
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DR EMBL; CP000518; ABL90552.1; -; Genomic_DNA.
DR AlphaFoldDB; A1UCJ4; -.
DR STRING; 189918.Mkms_1340; -.
DR KEGG; mkm:Mkms_1340; -.
DR HOGENOM; CLU_051152_0_0_11; -.
DR OrthoDB; 9788295at2; -.
DR UniPathway; UPA00071; -.
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 CDD; cd20607; FbiB_C-like; 1.
DR Gene3D; 3.30.1330.100; CofE-like; 1.
DR Gene3D; 3.90.1660.10; CofE-like domain; 1.
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 27..226
FT /note="Coenzyme F420:L-glutamate ligase-like"
FT /evidence="ECO:0000259|Pfam:PF01996"
FT DOMAIN 267..435
FT /note="Nitroreductase"
FT /evidence="ECO:0000259|Pfam:PF00881"
FT REGION 1..251
FT /note="Coenzyme F420:L-glutamate ligase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT REGION 252..455
FT /note="Dehydro-coenzyme F420-0 reductase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT REGION 433..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27..30
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 57
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 62
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 116
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 119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 157
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 158
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 267..271
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 295
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 327
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 406
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 443
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
SQ SEQUENCE 455 AA; 47920 MW; 5135883B3BDA2979 CRC64;
MTAHGGSAAP TDHGSAAAVE ILPVPGLPEF RPGDDLAAAL AAAAPWLRDG DVVVVTSKVV
SKCEGRIVAA PEDPEERDAL RRKLVDDEAV RVLARKGRTL ITENAIGLIQ AAAGVDGSNV
DTTELALLPV DPDGSAAHLR TGLAERLGVT VGIVITDTMG RAWRNGQIDA AIGAAGLAVL
HGYAGARDAH GNELLVTEVA VADEIAAAAD LVKGKLTGIP VAVVRGLTLA DNGSTAHDLL
RPGEDDLFWL GTEEAMAQGR AEAQLLRRSI RRFSADPVAP EMIEAAVAEA LTAPAPHHTR
PVRFVWVGDH ATRIRLLDRM KDRWRDDLLA DGLSADAVER RLARGQILYD APELVIPFLV
PDGAHDYPDD TRTAAEHTMF TVAVGAAVQA FLVALAVREV GSCWVGSTIF AADVVRAELD
LPAEWEPLGA VAVGHPAEPQ GPRDPVLPEG LLVRR
//
