FBVR_MYCTU
ID FBVR_MYCTU Reviewed; 137 AA.
AC P9WLL7; L0T8P9; Q10682;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=F420H(2)-dependent biliverdin reductase {ECO:0000303|PubMed:27364382};
DE Short=F-BVR {ECO:0000303|PubMed:27364382};
DE EC=1.3.98.- {ECO:0000269|PubMed:27364382};
GN OrderedLocusNames=Rv2074; ORFNames=MTCY49.13;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP PUPYLATION AT LYS-47, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA Gygi S.P., Darwin K.H.;
RT "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT tuberculosis.";
RL PLoS ONE 5:E8589-E8589(2010).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-137.
RC STRAIN=H37Rv;
RX PubMed=16880544; DOI=10.1107/s1744309106025012;
RA Biswal B.K., Au K., Cherney M.M., Garen C., James M.N.;
RT "The molecular structure of Rv2074, a probable pyridoxine 5'-phosphate
RT oxidase from Mycobacterium tuberculosis, at 1.6 angstroms resolution.";
RL Acta Crystallogr. F 62:735-742(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-135 IN COMPLEX WITH COENZYME
RP F420-3, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-21; TYR-104; TYR-108;
RP ARG-109; ARG-112 AND ARG-117, AND REACTION MECHANISM.
RX PubMed=27364382; DOI=10.1002/pro.2975;
RA Ahmed F.H., Mohamed A.E., Carr P.D., Lee B.M., Condic-Jurkic K.,
RA O'Mara M.L., Jackson C.J.;
RT "Rv2074 is a novel F420H2-dependent biliverdin reductase in Mycobacterium
RT tuberculosis.";
RL Protein Sci. 25:1692-1709(2016).
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:0000269|PubMed:27364382}.
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:0000269|PubMed:27364382};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.0 uM for biliverdin {ECO:0000269|PubMed:27364382};
CC Note=kcat is 0.072 sec(-1). {ECO:0000269|PubMed:27364382};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:27364382}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000305|PubMed:27364382}.
CC Secreted {ECO:0000305|PubMed:27364382}.
CC -!- SIMILARITY: Belongs to the F420H(2)-dependent biliverdin reductase
CC family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be an FMN-dependent pyridoxine 5'-
CC phosphate oxidase. {ECO:0000305|PubMed:16880544}.
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DR EMBL; AL123456; CCP44848.1; -; Genomic_DNA.
DR PIR; E70765; E70765.
DR RefSeq; NP_216590.1; NC_000962.3.
DR RefSeq; WP_003899157.1; NZ_NVQJ01000047.1.
DR PDB; 2ASF; X-ray; 1.60 A; A=2-137.
DR PDB; 5JAB; X-ray; 1.65 A; A/B/C/D=1-135.
DR PDBsum; 2ASF; -.
DR PDBsum; 5JAB; -.
DR AlphaFoldDB; P9WLL7; -.
DR SMR; P9WLL7; -.
DR STRING; 83332.Rv2074; -.
DR PaxDb; P9WLL7; -.
DR DNASU; 888523; -.
DR GeneID; 45426051; -.
DR GeneID; 888523; -.
DR KEGG; mtu:Rv2074; -.
DR PATRIC; fig|83332.111.peg.2312; -.
DR TubercuList; Rv2074; -.
DR eggNOG; COG3871; Bacteria.
DR OMA; ERHLCTL; -.
DR PhylomeDB; P9WLL7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0070967; F:coenzyme F420 binding; IDA:UniProtKB.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Isopeptide bond; Oxidoreductase; Reference proteome;
KW Secreted; Ubl conjugation.
FT CHAIN 1..137
FT /note="F420H(2)-dependent biliverdin reductase"
FT /id="PRO_0000103945"
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:0000269|PubMed:27364382"
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:0000269|PubMed:27364382"
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:0000269|PubMed:27364382"
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:0000269|PubMed:27364382"
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:0000269|PubMed:27364382"
FT CROSSLNK 47
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
FT MUTAGEN 21
FT /note="R->A: 2.7-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:27364382"
FT MUTAGEN 104
FT /note="Y->A: 17.8-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:27364382"
FT MUTAGEN 104
FT /note="Y->F: 8.9-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:27364382"
FT MUTAGEN 108
FT /note="Y->A: 44.5-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:27364382"
FT MUTAGEN 108
FT /note="Y->F: 3.3-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:27364382"
FT MUTAGEN 109
FT /note="R->A: 4.7-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:27364382"
FT MUTAGEN 112
FT /note="R->A: 2.6-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:27364382"
FT MUTAGEN 117
FT /note="R->A: 8.9-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:27364382"
FT HELIX 12..17
FT /evidence="ECO:0007829|PDB:2ASF"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:2ASF"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:2ASF"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:2ASF"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:2ASF"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:2ASF"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:2ASF"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:2ASF"
FT STRAND 80..91
FT /evidence="ECO:0007829|PDB:2ASF"
FT HELIX 94..107
FT /evidence="ECO:0007829|PDB:2ASF"
FT STRAND 117..129
FT /evidence="ECO:0007829|PDB:2ASF"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:2ASF"
SQ SEQUENCE 137 AA; 15024 MW; 1C6B531591EFEC8F CRC64;
MAMVNTTTRL SDDALAFLSE RHLAMLTTLR ADNSPHVVAV GFTFDPKTHI ARVITTGGSQ
KAVNADRSGL AVLSQVDGAR WLSLEGRAAV NSDIDAVRDA ELRYAQRYRT PRPNPRRVVI
EVQIERVLGS ADLLDRA
