ID   MENJ_MYCTO              Reviewed;         408 AA.
AC   P9WNY8; 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 47.
DE   RecName: Full=Menaquinone reductase {ECO:0000250|UniProtKB:P9WNY9};
DE            Short=MK reductase {ECO:0000250|UniProtKB:P9WNY9};
DE            EC=1.3.99.38 {ECO:0000250|UniProtKB:P9WNY9};
GN   Name=menJ {ECO:0000250|UniProtKB:P9WNY9}; OrderedLocusNames=MT0587;
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 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). {ECO:0000250|UniProtKB:P9WNY9}.
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:0000250|UniProtKB:P9WNY9};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q9HKS9};
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC       {ECO:0000250|UniProtKB:P9WNY9}.
CC   -!- SIMILARITY: Belongs to the geranylgeranyl reductase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK44810.1; -; Genomic_DNA.
DR   PIR; D70549; D70549.
DR   RefSeq; WP_003402939.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WNY8; -.
DR   SMR; P9WNY8; -.
DR   EnsemblBacteria; AAK44810; AAK44810; MT0587.
DR   KEGG; mtc:MT0587; -.
DR   PATRIC; fig|83331.31.peg.618; -.
DR   HOGENOM; CLU_024648_5_2_11; -.
DR   UniPathway; UPA00079; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
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; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   FAD; Flavoprotein; Menaquinone biosynthesis; Oxidoreductase.
FT   CHAIN           1..408
FT                   /note="Menaquinone reductase"
FT                   /id="PRO_0000427044"
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