ID A0A0A3YYZ7_9GAMM Unreviewed; 669 AA.
AC A0A0A3YYZ7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC {ECO:0000256|HAMAP-Rule:MF_01102};
DE Short=tRNA mnm(5)s(2)U biosynthesis bifunctional protein {ECO:0000256|HAMAP-Rule:MF_01102};
DE Includes:
DE RecName: Full=tRNA (mnm(5)s(2)U34)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01102};
DE EC=2.1.1.61 {ECO:0000256|HAMAP-Rule:MF_01102};
DE Includes:
DE RecName: Full=FAD-dependent cmnm(5)s(2)U34 oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01102};
DE EC=1.5.-.- {ECO:0000256|HAMAP-Rule:MF_01102};
GN Name=mnmC {ECO:0000256|HAMAP-Rule:MF_01102,
GN ECO:0000313|EMBL:KGT91845.1};
GN ORFNames=NG99_15890 {ECO:0000313|EMBL:KGT91845.1};
OS Erwinia typographi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=371042 {ECO:0000313|EMBL:KGT91845.1, ECO:0000313|Proteomes:UP000030351};
RN [1] {ECO:0000313|EMBL:KGT91845.1, ECO:0000313|Proteomes:UP000030351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M043b {ECO:0000313|EMBL:KGT91845.1,
RC ECO:0000313|Proteomes:UP000030351};
RA Chan K.-G., Tan W.-S.;
RT "Genome sequence of Erwinia typographi M043b.";
RL Submitted (OCT-2014) 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:0000256|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:0000256|HAMAP-
CC Rule:MF_01102};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01102};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01102}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the DAO family.
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_01102}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGT91845.1}.
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DR EMBL; JRUQ01000044; KGT91845.1; -; Genomic_DNA.
DR RefSeq; WP_034895003.1; NZ_JRUQ01000044.1.
DR AlphaFoldDB; A0A0A3YYZ7; -.
DR STRING; 371042.NG99_15890; -.
DR eggNOG; COG0665; Bacteria.
DR eggNOG; COG4121; Bacteria.
DR OrthoDB; 9786494at2; -.
DR Proteomes; UP000030351; Unassembled WGS sequence.
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)(34)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0002097; P:tRNA wobble base modification; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR047785; tRNA_MNMC2.
DR InterPro; IPR017610; tRNA_S-uridine_synth_MnmC_C.
DR NCBIfam; TIGR03197; MnmC_Cterm; 1.
DR NCBIfam; NF033855; tRNA_MNMC2; 1.
DR PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR13847:SF283; TRNA 5-METHYLAMINOMETHYL-2-THIOURIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN MNMC; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF05430; Methyltransf_30; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01102};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_01102};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_01102};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01102};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_01102};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01102};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01102};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01102};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01102}.
FT DOMAIN 119..244
FT /note="MnmC-like methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF05430"
FT DOMAIN 266..632
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT REGION 1..245
FT /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01102"
FT REGION 270..669
FT /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01102"
SQ SEQUENCE 669 AA; 73152 MW; 5F8939750F2B5465 CRC64;
MKTAPIEHAE LSWNEQGTPV SRAFGDVYFS NENGLEETRH VFLGGNQLPA RFAQHPRDLF
IAAETGFGTG LNFFTLWQAF DRFREAHPDA TLQRLHFISC EKYPLSAADL ASALANWPEL
AGYAAKLCER WPEALPGCHR LLLDGGRVTL DLWFGDINQL IHTFDDSLQQ QVDAWFLDGF
APSKNPDMWT PELFACMAKL ARKGATFATF TAAGFVRRGL QDAGFTVIRS KGFGPKREML
CGSLEQPLNT RAQLPWYSRP AAEGDDIAII GGGIASALLS LALLRRGKQV TLYCADAQAA
EGASGNRQGA LYPLLNQHDP ALARFFPAAF TFARRLYDSL PVTFDHDWCG VTQLGWDEKS
QQKIAKLRSM NLPKAIVREV STAEAEALCG VETGCGGMTW PSGGWLSPGQ LTPALVELAQ
QQGLRVCWQH TLSELIPTEA GWRLRFSSQP EQAHRNVVLA TGHTLASFAQ SEMLPAYAVS
GQVSHIPTTP GLNPLKQVLC YDGYLTPANP HNQHHCIGAS YHRADASTAY SAEDQQENRE
RLIRCLPKAN WAKEVDVSAG ESRSGVRCAS RDHLPMVGPL PDYQQTLAQY ADLAQHRDEV
PPAPVHQGLF VLGALGSRGL CSGPLGAEVL AAELCGEPIP LDADTLAALH PNRYWVRKLL
KGKAVKTAG
//
