F420R_MYCTU
ID F420R_MYCTU Reviewed; 147 AA.
AC O06553; L0T7G6;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=F420H(2)-dependent reductase Rv1155 {ECO:0000305|PubMed:27364382};
DE EC=1.-.-.- {ECO:0000269|PubMed:27364382};
GN OrderedLocusNames=Rv1155;
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 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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH FMN AND PYRIDOXAL
RP PHOSPHATE, AND SUBUNIT.
RX PubMed=16239726; DOI=10.1107/s0907444905026673;
RA Biswal B.K., Cherney M.M., Wang M., Garen C., James M.N.;
RT "Structures of Mycobacterium tuberculosis pyridoxine 5'-phosphate oxidase
RT and its complexes with flavin mononucleotide and pyridoxal 5'-phosphate.";
RL Acta Crystallogr. D 61:1492-1499(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND SUBUNIT.
RX PubMed=15620716; DOI=10.1016/j.febslet.2004.11.069;
RA Canaan S., Sulzenbacher G., Roig-Zamboni V., Scappuccini-Calvo L.,
RA Frassinetti F., Maurin D., Cambillau C., Bourne Y.;
RT "Crystal structure of the conserved hypothetical protein Rv1155 from
RT Mycobacterium tuberculosis.";
RL FEBS Lett. 579:215-221(2005).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-147 IN COMPLEX WITH COENZYME
RP F420-2, FUNCTION, COENZYME F420-BINDING, AND SUBUNIT.
RX PubMed=25644473; DOI=10.1002/pro.2645;
RA Mashalidis E.H., Gittis A.G., Tomczak A., Abell C., Barry C.E. III,
RA Garboczi D.N.;
RT "Molecular insights into the binding of coenzyme F420 to the conserved
RT protein Rv1155 from Mycobacterium tuberculosis.";
RL Protein Sci. 24:729-740(2015).
CC -!- FUNCTION: F420H(2)-dependent reductase able to catalyze the reduction
CC of biliverdin-IXalpha to bilirubin-IXalpha in vitro. However, kinetic
CC parameters show that it is less efficient than the biliverdin reductase
CC Rv2074 and suggest biliverdin-IXalpha is unlikely to be the native
CC substrate of Rv1155, which probably catalyzes the reduction of an
CC alternative molecule in vivo (PubMed:27364382). Binds coenzyme F420,
CC but does not bind FMN or other flavins (PubMed:25644473). Cannot use
CC pyridoxine 5'-phosphate, pyridoxamine 5'-phosphate, pyridoxal 5'-
CC phosphate (PLP), the anti-tuberculosis drug PA-824 or aflatoxin analogs
CC as substrates (PubMed:25644473). {ECO:0000269|PubMed:25644473,
CC ECO:0000269|PubMed:27364382}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=82.8 uM for biliverdin {ECO:0000269|PubMed:27364382};
CC Note=kcat is 0.024 sec(-1) for the reduction of biliverdin.
CC {ECO:0000269|PubMed:27364382};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15620716,
CC ECO:0000269|PubMed:16239726, ECO:0000269|PubMed:25644473}.
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:16239726}.
CC -!- CAUTION: FMN and PLP are seen in the crystal structures published in
CC PubMed:16239726, however, the enzyme does not bind these compounds in
CC vitro, and the complexes obtained in the crystal structures may be the
CC result of weak FMN/PLP binding that is stabilized by the crystal
CC lattice. {ECO:0000305|PubMed:25644473}.
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DR EMBL; AL123456; CCP43910.1; -; Genomic_DNA.
DR PIR; D70555; D70555.
DR RefSeq; NP_215671.1; NC_000962.3.
DR RefSeq; WP_003898745.1; NZ_NVQJ01000025.1.
DR PDB; 1W9A; X-ray; 1.80 A; A/B=1-147.
DR PDB; 1XXO; X-ray; 1.80 A; A/B=1-147.
DR PDB; 1Y30; X-ray; 2.20 A; A/B=1-147.
DR PDB; 2AQ6; X-ray; 1.70 A; A/B=1-147.
DR PDB; 4QVB; X-ray; 2.30 A; A/B=2-147.
DR PDBsum; 1W9A; -.
DR PDBsum; 1XXO; -.
DR PDBsum; 1Y30; -.
DR PDBsum; 2AQ6; -.
DR PDBsum; 4QVB; -.
DR AlphaFoldDB; O06553; -.
DR SMR; O06553; -.
DR STRING; 83332.Rv1155; -.
DR PaxDb; O06553; -.
DR DNASU; 885604; -.
DR GeneID; 885604; -.
DR KEGG; mtu:Rv1155; -.
DR TubercuList; Rv1155; -.
DR eggNOG; COG3467; Bacteria.
DR InParanoid; O06553; -.
DR OMA; DPRASYH; -.
DR PhylomeDB; O06553; -.
DR BRENDA; 1.4.3.5; 3445.
DR EvolutionaryTrace; O06553; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0070967; F:coenzyme F420 binding; IDA:UniProtKB.
DR GO; GO:0010181; F:FMN binding; IDA:MTBBASE.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:MTBBASE.
DR GO; GO:0042816; P:vitamin B6 metabolic process; IDA:MTBBASE.
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; Oxidoreductase; Reference proteome.
FT CHAIN 1..147
FT /note="F420H(2)-dependent reductase Rv1155"
FT /id="PRO_0000399901"
FT BINDING 32
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:25644473"
FT BINDING 37
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:25644473"
FT BINDING 50
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:25644473"
FT BINDING 56..60
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:25644473"
FT BINDING 77..79
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:25644473"
FT BINDING 138
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:25644473"
FT HELIX 6..15
FT /evidence="ECO:0007829|PDB:2AQ6"
FT STRAND 18..25
FT /evidence="ECO:0007829|PDB:2AQ6"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:2AQ6"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2AQ6"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:2AQ6"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:2AQ6"
FT HELIX 56..63
FT /evidence="ECO:0007829|PDB:2AQ6"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:2AQ6"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1W9A"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:2AQ6"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:2AQ6"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:2AQ6"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:2AQ6"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:2AQ6"
SQ SEQUENCE 147 AA; 16301 MW; DAF63639A04D6A0D CRC64;
MARQVFDDKL LAVISGNSIG VLATIKHDGR PQLSNVQYHF DPRKLLIQVS IAEPRAKTRN
LRRDPRASIL VDADDGWSYA VAEGTAQLTP PAAAPDDDTV EALIALYRNI AGEHSDWDDY
RQAMVTDRRV LLTLPISHVY GLPPGMR
