ID A0A2T6E4Q8_9GAMM Unreviewed; 651 AA.
AC A0A2T6E4Q8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ORFNames=BGP77_03340 {ECO:0000313|EMBL:PTY36352.1};
OS Saccharospirillum sp. MSK14-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Saccharospirillaceae; Saccharospirillum.
OX NCBI_TaxID=1897632 {ECO:0000313|EMBL:PTY36352.1, ECO:0000313|Proteomes:UP000244044};
RN [1] {ECO:0000313|EMBL:PTY36352.1, ECO:0000313|Proteomes:UP000244044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSK14-1 {ECO:0000313|EMBL:PTY36352.1,
RC ECO:0000313|Proteomes:UP000244044};
RA Nakajima Y., Yoshizawa S., Ogura Y., Hayashi T., Kogure K.;
RT "Draft genome of Saccharospirillum sp. MSK14-1.";
RL Submitted (AUG-2016) 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:PTY36352.1}.
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DR EMBL; MIES01000033; PTY36352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6E4Q8; -.
DR OrthoDB; 9786494at2; -.
DR Proteomes; UP000244044; 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; SSF54373; FAD-linked reductases, C-terminal domain; 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}; Reference proteome {ECO:0000313|Proteomes:UP000244044};
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 110..229
FT /note="MnmC-like methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF05430"
FT DOMAIN 259..618
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT REGION 1..231
FT /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01102"
FT REGION 262..651
FT /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01102"
SQ SEQUENCE 651 AA; 71086 MW; 04DE409A116B3350 CRC64;
MDTPLLETAA DGTPRSARFD DVYFSAAGGL DESRYVFINH NRLAERFAAL PEYGQFTVAE
TGFGTGLNCL AAWQLFQQLA PATARLTFIS TERYPLSAKQ IDTALAQWPE LAPLRHTLVR
QYPARFEGFH SVELADNVDL LLLFGDANVT LSELNAGVDA WFLDGFAPAK NPDLWQPTLF
DAMARLSRPN ASAATFTAAR RVRDGLSGAG FQVERVKGFG RKRDMVRAEY IGRCGPPRPG
LWPANEWVWP KTANQDRRAI VVGAGLAGAH SAWELAQRGW QVTVLEQATT VAAGASGNAQ
GAVYARLSAQ DAVANRFYSQ ALELSQQRLG QLPDSIPHAN CGLLQLNQGP KEAKRFQQYH
QANPYPADFV DLIAADKASE YAGVPLASDA LYFPNGGWVS PAALVAHRLD HPNIRVLTHH
TVSTLTPNDS GWQVDCDNGE RFNVPHVILA TAWQSAAFPQ TADLPLQPIA GQVSRIATTD
TLATLRAVLC SDRYLVPADR GLHSLGATFH LKQSQTDVRS EDDTDNLQSL HQRLPQLIQG
NETPVEARAG VRCASPDYLP LVGPVVNTQA FTTDYGEALR KRRTDRLPAP AHYPGLWVNI
AHGSKGLTTV PLTAKTLANG LNDEPMPIPQ NVLNQLNPNR FIIRQLIRGN A
//
