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   27-MAR-2024, entry version 135.
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; Actinomycetota; Actinomycetes; Mycobacteriales; 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.m111.011445;
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; 83332-Rv1155; -.
DR   DNASU; 885604; -.
DR   GeneID; 885604; -.
DR   KEGG; mtu:Rv1155; -.
DR   TubercuList; Rv1155; -.
DR   eggNOG; COG3467; Bacteria.
DR   InParanoid; O06553; -.
DR   OrthoDB; 1094370at2; -.
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   InterPro; IPR019920; F420-binding_dom_put.
DR   InterPro; IPR011576; Pyridox_Oxase_put.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   NCBIfam; TIGR03618; Rv1155_F420; 1.
DR   PANTHER; PTHR35176:SF2; F420H(2)-DEPENDENT REDUCTASE RV1155; 1.
DR   PANTHER; PTHR35176; HEME OXYGENASE HI_0854-RELATED; 1.
DR   Pfam; PF01243; Putative_PNPOx; 1.
DR   SUPFAM; SSF50475; FMN-binding split barrel; 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
//