FBVR_MYCTO
ID FBVR_MYCTO Reviewed; 137 AA.
AC P9WLL6; L0T8P9; Q10682;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=F420H(2)-dependent biliverdin reductase {ECO:0000250|UniProtKB:P9WLL7};
DE Short=F-BVR {ECO:0000250|UniProtKB:P9WLL7};
DE EC=1.3.98.- {ECO:0000250|UniProtKB:P9WLL7};
GN OrderedLocusNames=MT2134;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Catalyzes the F420H(2)-dependent reduction of biliverdin-
CC IXalpha at C10 position, leading to bilirubin-IXalpha, a potent
CC antioxidant. As biliverdin-IXalpha is produced in high amounts in
CC macrophages infected with M.tuberculosis, its reduction by Rv2074 may
CC play a role in protecting mycobacteria against oxidative stress, aiding
CC the persistence of M.tuberculosis infection.
CC {ECO:0000250|UniProtKB:P9WLL7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bilirubin IXalpha + H(+) + oxidized coenzyme F420-(gamma-L-
CC Glu)(n) = biliverdin IXalpha + reduced coenzyme F420-(gamma-L-
CC Glu)(n); Xref=Rhea:RHEA:56092, Rhea:RHEA-COMP:12939, Rhea:RHEA-
CC COMP:14378, ChEBI:CHEBI:15378, ChEBI:CHEBI:57977, ChEBI:CHEBI:57991,
CC ChEBI:CHEBI:133980, ChEBI:CHEBI:139511;
CC Evidence={ECO:0000250|UniProtKB:P9WLL7};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WLL7}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250|UniProtKB:P9WLL7}.
CC Secreted {ECO:0000250|UniProtKB:P9WLL7}.
CC -!- SIMILARITY: Belongs to the F420H(2)-dependent biliverdin reductase
CC family. {ECO:0000305}.
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DR EMBL; AE000516; AAK46414.1; -; Genomic_DNA.
DR PIR; E70765; E70765.
DR RefSeq; WP_003899157.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WLL6; -.
DR SMR; P9WLL6; -.
DR EnsemblBacteria; AAK46414; AAK46414; MT2134.
DR GeneID; 45426051; -.
DR KEGG; mtc:MT2134; -.
DR PATRIC; fig|83331.31.peg.2302; -.
DR HOGENOM; CLU_134364_0_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.30.110.10; -; 1.
DR InterPro; IPR019920; F420-binding_dom_put.
DR InterPro; IPR011576; Pyridox_Oxase_put.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR Pfam; PF01243; Putative_PNPOx; 1.
DR TIGRFAMs; TIGR03618; Rv1155_F420; 1.
PE 3: Inferred from homology;
KW Oxidoreductase; Secreted.
FT CHAIN 1..137
FT /note="F420H(2)-dependent biliverdin reductase"
FT /id="PRO_0000427457"
FT BINDING 36..41
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P9WLL7"
FT BINDING 54..55
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P9WLL7"
FT BINDING 60..61
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P9WLL7"
FT BINDING 67
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P9WLL7"
FT BINDING 78..81
FT /ligand="coenzyme F420-(gamma-Glu)n"
FT /ligand_id="ChEBI:CHEBI:133980"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P9WLL7"
SQ SEQUENCE 137 AA; 15024 MW; 1C6B531591EFEC8F CRC64;
MAMVNTTTRL SDDALAFLSE RHLAMLTTLR ADNSPHVVAV GFTFDPKTHI ARVITTGGSQ
KAVNADRSGL AVLSQVDGAR WLSLEGRAAV NSDIDAVRDA ELRYAQRYRT PRPNPRRVVI
EVQIERVLGS ADLLDRA
