MNMC_PSEAE
ID MNMC_PSEAE Reviewed; 654 AA.
AC Q9HYF0;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC {ECO:0000255|HAMAP-Rule:MF_01102};
DE Short=tRNA mnm(5)s(2)U biosynthesis bifunctional protein {ECO:0000255|HAMAP-Rule:MF_01102};
DE Includes:
DE RecName: Full=tRNA (mnm(5)s(2)U34)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01102};
DE EC=2.1.1.61 {ECO:0000255|HAMAP-Rule:MF_01102};
DE Includes:
DE RecName: Full=FAD-dependent cmnm(5)s(2)U34 oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01102};
DE EC=1.5.-.- {ECO:0000255|HAMAP-Rule:MF_01102};
GN Name=mnmC {ECO:0000255|HAMAP-Rule:MF_01102}; OrderedLocusNames=PA3456;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Catalyzes the last two steps in the biosynthesis of 5-
CC methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position
CC (U34) in tRNA. Catalyzes the FAD-dependent demodification of
CC cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl
CC group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form
CC mnm(5)s(2)U34. {ECO:0000255|HAMAP-Rule:MF_01102}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-
CC methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19569, Rhea:RHEA-
CC COMP:10195, Rhea:RHEA-COMP:10197, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74454,
CC ChEBI:CHEBI:74455; EC=2.1.1.61; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01102};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01102};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01102}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the methyltransferase
CC superfamily. tRNA (mnm(5)s(2)U34)-methyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_01102}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the DAO family.
CC {ECO:0000255|HAMAP-Rule:MF_01102}.
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DR EMBL; AE004091; AAG06844.1; -; Genomic_DNA.
DR PIR; G83213; G83213.
DR RefSeq; NP_252146.1; NC_002516.2.
DR RefSeq; WP_003114497.1; NZ_QZGE01000037.1.
DR AlphaFoldDB; Q9HYF0; -.
DR SMR; Q9HYF0; -.
DR STRING; 287.DR97_4465; -.
DR PaxDb; Q9HYF0; -.
DR PRIDE; Q9HYF0; -.
DR EnsemblBacteria; AAG06844; AAG06844; PA3456.
DR GeneID; 877843; -.
DR KEGG; pae:PA3456; -.
DR PATRIC; fig|208964.12.peg.3618; -.
DR PseudoCAP; PA3456; -.
DR HOGENOM; CLU_022427_1_0_6; -.
DR InParanoid; Q9HYF0; -.
DR OMA; NFLCAWQ; -.
DR PhylomeDB; Q9HYF0; -.
DR BioCyc; PAER208964:G1FZ6-3524-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016645; F:oxidoreductase activity, acting on the CH-NH group of donors; IEA:InterPro.
DR GO; GO:0004808; F:tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR HAMAP; MF_01102; MnmC; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR008471; MnmC-like_methylTransf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR023032; tRNA_MAMT_biosynth_bifunc_MnmC.
DR InterPro; IPR017610; tRNA_S-uridine_synth_MnmC_C.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF05430; Methyltransf_30; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR03197; MnmC_Cterm; 1.
PE 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; Methyltransferase; Multifunctional enzyme;
KW Oxidoreductase; Reference proteome; S-adenosyl-L-methionine; Transferase;
KW tRNA processing.
FT CHAIN 1..654
FT /note="tRNA 5-methylaminomethyl-2-thiouridine biosynthesis
FT bifunctional protein MnmC"
FT /id="PRO_0000095021"
FT REGION 1..235
FT /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT REGION 261..654
FT /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
SQ SEQUENCE 654 AA; 70518 MW; 8E8B55792B94BF0E CRC64;
MSDFQHAQLD WDENGQPLSR AFGDVYFSRH SGLNETRHVF LATNRLAERF AALGDGEVLC
IGETGFGTGL NFLCAWQLFE RVAPAGARLE FVSVEKFPLA AADLRRALAL WPELAPWSEA
LLGQYLAVHP GFQRLAFAGG RVGLTLLLGD ALECLPQLDA RVDAWFLDGF APAKNPDMWS
PVLFAELARL SAPQATLGTF TSAGFVRRGL VEAGFAMQRV PGYGQKREML SGTYQGPPAN
AGKPWYARPA PHAGRRAALV VGGGLAGCAS AASLAARGWQ VTLIERHPGL AREASGNPQG
VLYLKLSAHG TPLSRLVLSG FGHTRRLLER LRRGHDWDAC GVLQLAFDAK EAQRQAQLAA
AFPADLLHGL EREQAERLAG VALPAGGLFY PEAGWVHPPA LCQALAATPG ITLLSGRAVR
LRREGDDWCA YAGDECLARA PLAILATAAD IRDFPPAAEL PLKRIRGQVT RLPATPQSRA
LRTVVCAEGY VAPPRGDEHT LGASFDFKSE DLAPTLAEHQ GNLELLREIS PDLLQRLGAD
DLPLERLEGR AAFRCTSPDY LPLVGPLAER AAFDEAYAVL ARDARQVPER ACPWLPGLYL
NSGHGSRGLI SAPLSGELLA AWICGEPLPL PRAVAEACHP NRFLLRDLVR GQRG
