MNMC_SHEAM
ID MNMC_SHEAM Reviewed; 665 AA.
AC A1S7K4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 25-MAY-2022, entry version 70.
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=Sama_2155;
OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=326297;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1098 / SB2B;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA Richardson P.;
RT "Complete sequence of Shewanella amazonensis SB2B.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABM00361.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000507; ABM00361.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A1S7K4; -.
DR SMR; A1S7K4; -.
DR STRING; 326297.Sama_2155; -.
DR EnsemblBacteria; ABM00361; ABM00361; Sama_2155.
DR KEGG; saz:Sama_2155; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_451910_0_0_6; -.
DR Proteomes; UP000009175; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-EC.
DR GO; GO:0002097; P:tRNA wobble base modification; IEA:UniProtKB-UniRule.
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; IPR023032; tRNA_MAMT_biosynth_bifunc_MnmC.
DR InterPro; IPR017610; tRNA_S-uridine_synth_MnmC_C.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; SSF51905; 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..665
FT /note="tRNA 5-methylaminomethyl-2-thiouridine biosynthesis
FT bifunctional protein MnmC"
FT /id="PRO_0000348022"
FT REGION 1..243
FT /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT REGION 264..665
FT /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
SQ SEQUENCE 665 AA; 72346 MW; 3EF0DF3B01CC7507 CRC64;
MSDSVTSCLL LPILETMPMP VITTLFMFYY PFRTGSTNFS APIVSPLALL SGQLSIKGGK
IMPISRHRVN FFNPMPEFFA IDMAMPLSLP LPEGPCVVLF EALPEPPLWQ WLLAAAQVNS
AYPETNAAYA SNASITSIQH TSKKPLQIIM LLKDEAELNA LAMDASHPLS PFAMAASHIK
GGQRFHLDDN CWLDFYLCEP NKAATLATFD KASIDVLICP KGEFEQAALE LAHQGSILIG
DTKPDMPAAL PIKPPFKPRD ISIVGAGVAG ASLALSLLRR GHKVTLYCAD AAPGIGASGN
RQGAIYPLLT PEDDHLTRLF VPAFLYAKRF VESLAHHPLP FDFCGVLQTG HDERATERIE
KLLSKTWPKQ VAVRVDADEA NHIAGVAIDK GGIYYPQGGW VSPAKLCEAA IEEAKTMGLE
CHFDVNITSI TRADEGWRLN TQTGEIDAHE LVLATGHRIT ELAQTKSLQL APFRGQVSHV
PTRGKLEQLK TVLCAHGYFT PRDASSGSHC MGASYVRGDT SVEYREQEQQ ENLHKMQESY
PGKDWVEYLD ISEGSARAGI RMVSRDHLPM AGAAPDVAAI QTQYQAIGHG PKGAQYWQTH
AAPVHPGLYI FSGLGSRGLS SGPLIAECLA DSLSGTLPVL DGDVMEALNP NRMWLRKLKK
GKALD
