ID W5TPL2_9NOCA Unreviewed; 452 AA.
AC W5TPL2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=cofE {ECO:0000313|EMBL:AHH21094.1};
GN Synonyms=fbiB {ECO:0000256|HAMAP-Rule:MF_01259};
GN ORFNames=NONO_c63240 {ECO:0000313|EMBL:AHH21094.1};
OS Nocardia nova SH22a.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH21094.1, ECO:0000313|Proteomes:UP000019150};
RN [1] {ECO:0000313|EMBL:AHH21094.1, ECO:0000313|Proteomes:UP000019150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH22a {ECO:0000313|EMBL:AHH21094.1};
RX PubMed=24747905;
RA Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.;
RT "Insights into the Microbial Degradation of Rubber and Gutta-Percha by
RT Analysis of the Complete Genome of Nocardia nova SH22a.";
RL Appl. Environ. Microbiol. 80:3895-3907(2014).
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}.
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DR EMBL; CP006850; AHH21094.1; -; Genomic_DNA.
DR RefSeq; WP_025352423.1; NZ_CP006850.1.
DR AlphaFoldDB; W5TPL2; -.
DR STRING; 1415166.NONO_c63240; -.
DR KEGG; nno:NONO_c63240; -.
DR PATRIC; fig|1415166.3.peg.6496; -.
DR eggNOG; COG0778; Bacteria.
DR eggNOG; COG1478; Bacteria.
DR HOGENOM; CLU_051152_0_0_11; -.
DR OrthoDB; 9788295at2; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000019150; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000019150}.
FT DOMAIN 24..223
FT /note="Coenzyme F420:L-glutamate ligase-like"
FT /evidence="ECO:0000259|Pfam:PF01996"
FT DOMAIN 264..432
FT /note="Nitroreductase"
FT /evidence="ECO:0000259|Pfam:PF00881"
FT REGION 1..248
FT /note="Coenzyme F420:L-glutamate ligase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT REGION 249..452
FT /note="Dehydro-coenzyme F420-0 reductase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 24..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 54
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 59
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 113
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 116
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 154
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 155
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 264..268
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 292
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 324
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 403
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
FT BINDING 440
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01259"
SQ SEQUENCE 452 AA; 48004 MW; 0F797AA21F5AF63D CRC64;
MSEQARAGDH APGGEVRIIP VPGLPEFRPG DDVAEHIAAQ APWLADGDVL VVTSKIVAKA
EGRIVAAPLD PEERDAVRRK LVDAEAVRVL ARKGRTLITE NRIGIVQAAS GVDGSNVEQG
ELVLLPTDPD ASAKAIRSEL ARRLGVEVAV VITDTMGRAW RIGQIDAAIG AAGLRVVHDY
AGAVDGQGNE LQVTQVAVAD ELAAAADLAK GKLGGVPVAV VRGLATVDDG STAKDLLRGG
EEDLFWLGTA EAIERGRREA LLVRRSVRSF AATPVEPELI RAAVADALTA PAPHHTHPVR
FVWVREPELR ARLLNAMAAR WRDDLGGDGL APERVERRVA RGRILFDAPE VIIPFCVPDG
AHDYPDQRRR AAESTMFTVA VGAAVQGLLV ALATRGVGSC WIGSTIFAPE VTREVLDLAG
DWNPLGAIAV GYPEEELQPR EPRPGGFGLI EL
//
