MNMC_ACIBC
ID MNMC_ACIBC Reviewed; 623 AA.
AC B2HYP8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=ACICU_03175;
OS Acinetobacter baumannii (strain ACICU).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=405416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACICU;
RX PubMed=18411315; DOI=10.1128/aac.01643-07;
RA Iacono M., Villa L., Fortini D., Bordoni R., Imperi F., Bonnal R.J.,
RA Sicheritz-Ponten T., De Bellis G., Visca P., Cassone A., Carattoli A.;
RT "Whole-genome pyrosequencing of an epidemic multidrug-resistant
RT Acinetobacter baumannii strain belonging to the European clone II group.";
RL Antimicrob. Agents Chemother. 52:2616-2625(2008).
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; CP000863; ACC58487.1; -; Genomic_DNA.
DR RefSeq; WP_001043531.1; NZ_CP031380.1.
DR AlphaFoldDB; B2HYP8; -.
DR SMR; B2HYP8; -.
DR KEGG; abc:ACICU_03175; -.
DR HOGENOM; CLU_022427_2_0_6; -.
DR OMA; NFLCAWQ; -.
DR Proteomes; UP000008839; 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; 3.40.50.150; -; 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 TIGRFAMs; TIGR03197; MnmC_Cterm; 1.
PE 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; Methyltransferase; Multifunctional enzyme;
KW Oxidoreductase; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..623
FT /note="tRNA 5-methylaminomethyl-2-thiouridine biosynthesis
FT bifunctional protein MnmC"
FT /id="PRO_0000347933"
FT REGION 1..244
FT /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT REGION 270..623
FT /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
SQ SEQUENCE 623 AA; 70155 MW; 61DAC0A4539FEB73 CRC64;
MNKSNRIQTA ELDWESIDGI EVPISKQFGD VYFSKDNGLL ETRHVFLNGN DLSERLANLQ
DFEYFSVGET GFGTGLNILA LWQLWQQVRP NNHSHLHAIS VEKFPLSKAD LIRALNVWDE
LRPLSKQLIE QYPFPLAGCH RLSFPEERFS IDLWLGDAQD IFPSMVKTKA VNAWFLDGFA
PSCNPDMWEQ NVLNNIVRLS DYGTTFASFS VAGILKRGLK AHGVDITRPR GFGHKREMLK
AVWKAPVSEE ILLEPVRDTF QFTQQRIAVI GAGIAGLSTA WAFAQRGHQV TLFERTVPLS
GASGNPLALL NPKLCPIEQS HEHLMTLSWQ HALNFYKNFQ AFRPIQIQQM ALKNAQDLLD
LADQYPADIV TQQTSSLESD YPHILLTEAG AVSPHQLRDE ILQHPGIELK IANITTLISF
ENKVQLKSGN ETTLEADHVV VCCARESAAL FENYPLLKPI RGQVSWVDNS FATLPLNEAY
SYGGYCMQLN TSELILGASF YPNRDDQEVL LDDHVHNFEL IHSVFPHYAK QLPPVEQWQG
RASVRAQSPD YFPLVGKMQN ESRISTFAGL GSKGFLFAPL CSEVLVAQIL GEACPVPKSL
LQKLDAQRFQ KKVKPKKPYF KSQ
