ID   MENJ_MYCTU              Reviewed;         408 AA.
AC   P9WNY9; F2GMK6; L0T5R0; O06427; Q7D9M7;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Menaquinone reductase {ECO:0000303|PubMed:26436137};
DE            Short=MK reductase {ECO:0000303|PubMed:26436137};
DE            EC=1.3.99.38 {ECO:0000269|PubMed:26436137};
GN   Name=menJ {ECO:0000303|PubMed:26436137}; OrderedLocusNames=Rv0561c;
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   INDUCTION.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=22485172; DOI=10.1371/journal.pone.0034471;
RA   Schuessler D.L., Parish T.;
RT   "The promoter of Rv0560c is induced by salicylate and structurally-related
RT   compounds in Mycobacterium tuberculosis.";
RL   PLoS ONE 7:E34471-E34471(2012).
RN   [4]
RP   IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND
RP   PATHWAY.
RC   STRAIN=H37Rv;
RX   PubMed=26436137; DOI=10.1021/acscentsci.5b00212;
RA   Upadhyay A., Fontes F.L., Gonzalez-Juarrero M., McNeil M.R., Crans D.C.,
RA   Jackson M., Crick D.C.;
RT   "Partial saturation of menaquinone in Mycobacterium tuberculosis: function
RT   and essentiality of a novel reductase, MenJ.";
RL   ACS Cent. Sci. 1:292-302(2015).
CC   -!- FUNCTION: Catalyzes the reduction of a single double bond in the
CC       isoprenoid tail of menaquinone (MK-9) in M.tuberculosis, likely the
CC       beta-isoprene unit, forming the predominant form of menaquinone found
CC       in mycobacteria, MK-9(II-H2). Is required for M.tuberculosis survival
CC       in host macrophages. {ECO:0000269|PubMed:26436137}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + menaquinone-9 = A + beta-dihydromenaquinone-9;
CC         Xref=Rhea:RHEA:51924, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:44147, ChEBI:CHEBI:134607; EC=1.3.99.38;
CC         Evidence={ECO:0000269|PubMed:26436137};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q9HKS9};
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC       {ECO:0000269|PubMed:26436137}.
CC   -!- INDUCTION: Constitutively expressed at a low level, not induced by
CC       salicylate. {ECO:0000269|PubMed:22485172}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene show complete abolition
CC       of the synthesis of MK-9(II-H2) accompanied by accumulation of MK-9.
CC       They have similar growth rates than wild-type in both aerated and
CC       hypoxic culture conditions. However, despite having similar levels of
CC       adhesion and infection at the earliest time point, the survival of
CC       mutant bacilli in the macrophages is dramatically reduced.
CC       {ECO:0000269|PubMed:26436137}.
CC   -!- SIMILARITY: Belongs to the geranylgeranyl reductase family.
CC       {ECO:0000305}.
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DR   EMBL; AL123456; CCP43299.1; -; Genomic_DNA.
DR   PIR; D70549; D70549.
DR   RefSeq; NP_215075.1; NC_000962.3.
DR   RefSeq; WP_003402939.1; NZ_NVQJ01000036.1.
DR   AlphaFoldDB; P9WNY9; -.
DR   SMR; P9WNY9; -.
DR   STRING; 83332.Rv0561c; -.
DR   PaxDb; P9WNY9; -.
DR   DNASU; 887638; -.
DR   GeneID; 887638; -.
DR   KEGG; mtu:Rv0561c; -.
DR   TubercuList; Rv0561c; -.
DR   eggNOG; COG0644; Bacteria.
DR   OMA; SLCDPFL; -.
DR   PhylomeDB; P9WNY9; -.
DR   BioCyc; MetaCyc:G185E-4694-MON; -.
DR   BRENDA; 1.3.99.38; 3445.
DR   UniPathway; UPA00079; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IMP:UniProtKB.
DR   GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IMP:UniProtKB.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR011777; Geranylgeranyl_Rdtase_fam.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR02032; GG-red-SF; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Menaquinone biosynthesis; Oxidoreductase;
KW   Reference proteome; Virulence.
FT   CHAIN           1..408
FT                   /note="Menaquinone reductase"
FT                   /id="PRO_0000419774"
FT   BINDING         13..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HKS9"
FT   BINDING         46..49
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HKS9"
FT   BINDING         103
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HKS9"
FT   BINDING         127
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HKS9"
FT   BINDING         290
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HKS9"
FT   BINDING         302..303
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HKS9"
SQ   SEQUENCE   408 AA;  43870 MW;  B2F61E46A656EA8C CRC64;
     MSVDDSADVV VVGAGPAGSA AAAWAARAGR DVLVIDTATF PRDKPCGDGL TPRAVAELHQ
     LGLGKWLADH IRHRGLRMSG FGGEVEVDWP GPSFPSYGSA VARLELDDRI RKVAEDTGAR
     MLLGAKAVAV HHDSSRRVVS LTLADGTEVG CRQLIVADGA RSPLGRKLGR RWHRETVYGV
     AVRGYLSTAY SDDPWLTSHL ELRSPDGAVL PGYGWIFPLG NGEVNIGVGA LSTSRRPADL
     ALRPLISYYT DLRRDEWGFT GQPRAVSSAL LPMGGAVSGV AGSNWMLIGD AAACVNPLNG
     EGIDYGLETG RLAAELLDSR DLARLWPSLL ADRYGRGFSV ARRLALLLTF PRFLPTTGPI
     TMRSTALMNI AVRVMSNLVT DDDRDWVARV WRGGGQLSRL VDRRPPFS