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MNMC_PSYWF
ID   MNMC_PSYWF              Reviewed;         739 AA.
AC   A5WGY8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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};
GN   OrderedLocusNames=PsycPRwf_1989;
OS   Psychrobacter sp. (strain PRwf-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=349106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRwf-1;
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter sp. PRwf-1.";
RL   Submitted (MAY-2007) 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; CP000713; ABQ94929.1; -; Genomic_DNA.
DR   RefSeq; WP_011961203.1; NC_009524.1.
DR   AlphaFoldDB; A5WGY8; -.
DR   SMR; A5WGY8; -.
DR   STRING; 349106.PsycPRwf_1989; -.
DR   EnsemblBacteria; ABQ94929; ABQ94929; PsycPRwf_1989.
DR   KEGG; prw:PsycPRwf_1989; -.
DR   eggNOG; COG0665; Bacteria.
DR   eggNOG; COG4121; Bacteria.
DR   HOGENOM; CLU_022427_1_0_6; -.
DR   OMA; NFLCAWQ; -.
DR   OrthoDB; 912110at2; -.
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..739
FT                   /note="tRNA 5-methylaminomethyl-2-thiouridine biosynthesis
FT                   bifunctional protein MnmC"
FT                   /id="PRO_0000348016"
FT   REGION          1..282
FT                   /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT   REGION          330..739
FT                   /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
SQ   SEQUENCE   739 AA;  81423 MW;  D807B69BFAF5E741 CRC64;
     MDKVTPAKLS WREDELGNVV PVSEIFGDVY YSLVDGLNES RYVFLTQNKL PERFEALFSR
     ANSSAASNFS IAELGFGTGL NILATWQLWE HSKQQFHTYF NSQTNLQTSS QDHLKGSRSL
     TPRLHIISTE KHPLTHADLS RSLESWKHKD TSLVPFVDQL LALYPTLISG CHRLQLAEDV
     TLDLWLGDAC FSLQQLANSY DTLPYGAHID AWYLDGFAPA CNESLWADQI FEQVKRLSKP
     GTTAATFSSA GVVKRGLMAA GFEIKKTKGF GRKREMLTAT KLEPVAVSDD TSDNQGATEY
     DAKSTLALRS KEQVTLDTHA VTPNEQIAVI GAGVCGLMAA WSLAQRGNAV SLIDKEAPLA
     GASGNPRALL APKMTPLAHV AEHLHSISYL YSQRFYRQID QGEHKIFTPT TTLDLLQKSN
     VDVHQIAEYP EQMATTLSLD SARDISGLQQ QDLTANLYLP QSGLINPKAL ADKVLTHPNI
     SFKQANIKRI TPLQAEAFDD VTEVSEVIEV TADITVQPAK RTKVMLHCES GEVLSVNRVV
     IAAAFESQSL DARIFEFRKI RGQLSWFEPT TEQLQALPTL PLKYSGYCAP FIPQPGDEAV
     NSVTPSVPTF LLGASFIRND LDDEIRLSEH AINHQKLLTA LPELSAVLPL PDTEADLYQR
     WQARVGIRSQ TPDYHPLVGA VDEQGLIWTL SGMGSKGYAF APLCAQVLAD MMTAQFVPLP
     AALLAKLSVH RSSLKKPLS
 
 
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