MNMC_SHEWM
ID MNMC_SHEWM Reviewed; 696 AA.
AC B1KKR3;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=Swoo_3009;
OS Shewanella woodyi (strain ATCC 51908 / MS32).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=392500;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51908 / MS32;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella woodyi ATCC 51908.";
RL Submitted (FEB-2008) 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}.
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DR EMBL; CP000961; ACA87280.1; -; Genomic_DNA.
DR RefSeq; WP_012325616.1; NC_010506.1.
DR AlphaFoldDB; B1KKR3; -.
DR SMR; B1KKR3; -.
DR STRING; 392500.Swoo_3009; -.
DR EnsemblBacteria; ACA87280; ACA87280; Swoo_3009.
DR KEGG; swd:Swoo_3009; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_022427_2_1_6; -.
DR OMA; MGCAPDF; -.
DR OrthoDB; 912110at2; -.
DR Proteomes; UP000002168; 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..696
FT /note="tRNA 5-methylaminomethyl-2-thiouridine biosynthesis
FT bifunctional protein MnmC"
FT /id="PRO_0000348038"
FT REGION 1..262
FT /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT REGION 287..696
FT /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
SQ SEQUENCE 696 AA; 77215 MW; 62C05429BD8D0F01 CRC64;
MPNMRRRVNS LAQECEKNTQ MNQETANFSE FYRLLSNIAV GKQSLTFGQL GLGSVEQLLA
VHSWLSSAPT SVRIKLKVFE AQLDTLPLFI SQLSSYTPPS SKQGSFIQTL TEADPIEILG
CQRLIFDDGR FVIDLYLNSP IASLKSMRLP TCDGSDDDKS PLFDLWTISQ TNSNRVESGM
EQEISQALLW QVAKVSQDSA PVYNFNLKQG KEIRQLCQKT GFSLISYRSQ NEEMTPKLTS
DLSSLDTQIC LQERKALRHA QAQDSLYTPV GQASSETDSE SDTFAIIGGG VASAHLALSL
AQRNKTVRLF CNDSSLAQQA SGNKQGAVYP LLTPDNGHLS HYYQQGYLFS RRRLQSLIKD
GFKVGYDFCG VLQTGFDQRS SARLEKIITA QPWNKQIAHG VDRHESSNLA GIDIDKAGIF
YPLGGWICPH EFTQAAFDKA SQLSDVSAHF NTDIKRIEQR EGKWYLHKTT VNTGGEQTFG
PFNTLILANG QGLNQFNQSK QLAATGFRGQ VSHIPARNEL LKLNTVLCSH GYLTPQNDGV
HCTGASYIKN PEHLDYSPSE QAENLEKVKQ SYLGKAWTED VDISDHSARV GVRMVTRDHA
PMMGCAPDFD VISLNYQNHQ HTKESIKYWR ETPAPIHQGL FILGGLGSRG ITSGPLAAEA
LAAQLCGEII PLDNATLELL NPNRMWMRKL IKGKAL
