FBIB_KITAU
ID FBIB_KITAU Reviewed; 429 AA.
AC Q75UN0;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 77.
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};
DE EC=6.3.2.34 {ECO:0000255|HAMAP-Rule:MF_01259};
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:0000255|HAMAP-Rule:MF_01259};
DE EC=1.3.8.17 {ECO:0000255|HAMAP-Rule:MF_01259};
GN Name=fbiB {ECO:0000255|HAMAP-Rule:MF_01259}; Synonyms=tchA;
OS Kitasatospora aureofaciens (Streptomyces aureofaciens).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Kitasatospora.
OX NCBI_TaxID=1894;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HP77;
RX PubMed=15215601; DOI=10.1271/bbb.68.1345;
RA Nakano T., Miyake K., Endo H., Dairi T., Mizukami T., Katsumata R.;
RT "Identification and cloning of the gene involved in the final step of
RT chlortetracycline biosynthesis in Streptomyces aureofaciens.";
RL Biosci. Biotechnol. Biochem. 68:1345-1352(2004).
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:0000255|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:0000255|HAMAP-
CC 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:0000255|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:0000255|HAMAP-
CC Rule:MF_01259};
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 -!- 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}.
CC -!- CAUTION: Was originally (PubMed:15215601) thought to be a probable
CC tetracycline dehydrogenase since it is essential to the final reaction
CC in the biosynthesis of 6-demethyltetracycline, but enzymatic activity
CC has not been proven. Several facts suggest it is more likely to be a
CC coenzyme F420:L-glutamate ligase: it is a homolog of the characterized
CC protein CofE from Methanococcus jannaschii and FbiB from Mycobacterium
CC smegmatis which are involved in the polyglutamylation of F420-0; F420
CC is used for tetracycline biosynthesis, probably being necessary for the
CC last step; the gene coding for this protein is close to a homolog of
CC the characterized protein CofD from Methanococcus jannaschii involved
CC in F420-0 production. {ECO:0000305|PubMed:15215601}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD16617.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB125899; BAD16617.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; Q75UN0; -.
DR SMR; Q75UN0; -.
DR STRING; 1894.JOER01000062_gene89; -.
DR eggNOG; COG0778; Bacteria.
DR eggNOG; COG1478; Bacteria.
DR UniPathway; UPA00071; -.
DR GO; GO:0052618; F:coenzyme F420-0:L-glutamate ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0052619; F:coenzyme F420-1:gamma-L-glutamate ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
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; 2.
DR Pfam; PF00881; Nitroreductase; 1.
DR SUPFAM; SSF55469; SSF55469; 1.
DR TIGRFAMs; TIGR01916; F420_cofE; 1.
DR TIGRFAMs; TIGR03553; F420_FbiB_CTERM; 1.
PE 3: Inferred from homology;
KW GTP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW Multifunctional enzyme; Nucleotide-binding; Oxidoreductase; Potassium.
FT CHAIN 1..429
FT /note="Bifunctional F420 biosynthesis protein FbiB"
FT /id="PRO_0000145782"
FT REGION 1..229
FT /note="Coenzyme F420:L-glutamate ligase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
FT REGION 230..429
FT /note="Dehydro-coenzyme F420-0 reductase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
FT BINDING 11..14
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
FT BINDING 40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
FT BINDING 45
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
FT BINDING 91
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 94
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
FT BINDING 132
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 133
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 269
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
FT BINDING 301
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
FT BINDING 381
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
FT BINDING 418
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01259"
SQ SEQUENCE 429 AA; 45624 MW; 1384FB51586DD823 CRC64;
MALEILGVEG IPEVDAGADL AGLIAKAGTY RDGDILLVTS KVVSKAEGRL LHAADRDAAI
DAETVRVVAR RGPARIVENR NGFVMAAAGV DASNTAPGTV LLLPEDPDAS ARALRSRLQQ
LTGCRLAVVV TDTFGRPWRN GLTDVAIGAA GLSVLEDHRG RTDSHGNELV LTVTATADEL
AAAADLVKGK ATGVPVAIVR GLGHLVTAED GAGTRPLVRA AADDMFRLGT SEALRQAVTL
RRTVRSFTTD PVDPAAVRRA VAAAVTAPAP HHTTPWRFVL LESAGTRVRL LDAMLGAWQR
DLRELDGWDE ARIARRTARG DVLRDAPYLV VPCLVMDGSH DYPDPRRAAA EREMFTVAAG
AGVQNLLVAL TGEGYGSAWV SSTMFCRDTV REVLDLPEGW DPMGAVAVGR PAEVPRERRR
EAEAFVEVR
