MENJ_MYCS2
ID MENJ_MYCS2 Reviewed; 409 AA.
AC A0QRI8;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 108.
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};
GN OrderedLocusNames=MSMEG_1132 {ECO:0000312|EMBL:ABK72592.1},
GN MSMEI_1100 {ECO:0000312|EMBL:AFP37578.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
RC STRAIN=ATCC 700084 / mc(2)155;
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.smegmatis, likely the beta-
CC isoprene unit, forming the predominant form of menaquinone found in
CC mycobacteria, MK-9(II-H2). {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 -!- 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, mycobacterial electron transport
CC efficiency is reduced by 3-fold in mutant cells, but mycobacteria are
CC able to maintain ATP levels by increasing the levels of the total
CC menaquinone in the membrane. Proton motive force (PMF) and oxidative
CC phosphorylation are not affected. {ECO:0000269|PubMed:26436137}.
CC -!- SIMILARITY: Belongs to the geranylgeranyl reductase family.
CC {ECO:0000305}.
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DR EMBL; CP000480; ABK72592.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37578.1; -; Genomic_DNA.
DR RefSeq; YP_885526.1; NC_008596.1.
DR AlphaFoldDB; A0QRI8; -.
DR SMR; A0QRI8; -.
DR STRING; 246196.MSMEI_1100; -.
DR EnsemblBacteria; ABK72592; ABK72592; MSMEG_1132.
DR EnsemblBacteria; AFP37578; AFP37578; MSMEI_1100.
DR KEGG; msg:MSMEI_1100; -.
DR KEGG; msm:MSMEG_1132; -.
DR PATRIC; fig|246196.19.peg.1124; -.
DR eggNOG; COG0644; Bacteria.
DR OMA; SLCDPFL; -.
DR OrthoDB; 1770293at2; -.
DR BRENDA; 1.3.99.38; 3512.
DR UniPathway; UPA00079; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
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.
FT CHAIN 1..409
FT /note="Menaquinone reductase"
FT /id="PRO_0000435885"
FT BINDING 11..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HKS9"
FT BINDING 44..47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HKS9"
FT BINDING 101
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HKS9"
FT BINDING 125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HKS9"
FT BINDING 288
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HKS9"
FT BINDING 300..301
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HKS9"
SQ SEQUENCE 409 AA; 43404 MW; E4210F54EA9679A9 CRC64;
MNTRADVVVV GAGPAGSAAA AWAARAGRDV VVVDAAQFPR DKACGDGLTP RAVAELQRLG
MASWLDTRIR HHGLRMSGFG ADVEIPWPGP SFPATSSAVP RTELDDRIRS VAADDGAKMM
LGTKVVDVTH DSSGRVDAVV LDDGNTVGCA QLIVADGARS TLGRVLGRTW HRETVYGVAI
RGYIASPRAS EPWITSHLEL RSPEGKVLPG YGWMFPLGNG EVNIGVGALA TAKRPADAAL
RPLMSYYADL RREEWGLVGE PRAGLSALLP MGGAVSGVAG PNWMLIGDAA ACVNPLNGEG
IDYGLETGRL AAELMTSGGV TDYSSAWPTL LQEHYARGFS VARRLALLLT LPRFLQVTGP
VAMRSATLMT IAVRVMGNLV TDEDADWIAR VWRTAGLASR RIDQRVPFS
