ID A0A0A3W8Q4_9GAMM Unreviewed; 632 AA.
AC A0A0A3W8Q4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=GW12_05440 {ECO:0000313|EMBL:KGT48421.1};
OS Acinetobacter sp. HR7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1509403 {ECO:0000313|EMBL:KGT48421.1, ECO:0000313|Proteomes:UP000032870};
RN [1] {ECO:0000313|EMBL:KGT48421.1, ECO:0000313|Proteomes:UP000032870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR7 {ECO:0000313|EMBL:KGT48421.1,
RC ECO:0000313|Proteomes:UP000032870};
RA Ahn S., Kim B.-C.;
RT "Genome sequencing of Acinetobacter sp. strain HR7.";
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:KGT48421.1}.
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DR EMBL; JPQO01000042; KGT48421.1; -; Genomic_DNA.
DR RefSeq; WP_034583149.1; NZ_JPQO01000042.1.
DR AlphaFoldDB; A0A0A3W8Q4; -.
DR STRING; 1509403.GW12_05440; -.
DR PATRIC; fig|1509403.3.peg.538; -.
DR eggNOG; COG0665; Bacteria.
DR eggNOG; COG4121; Bacteria.
DR OrthoDB; 9786494at2; -.
DR Proteomes; UP000032870; 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; SSF51971; Nucleotide-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 117..240
FT /note="MnmC-like methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF05430"
FT DOMAIN 274..595
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT REGION 1..242
FT /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01102"
FT REGION 277..632
FT /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01102"
SQ SEQUENCE 632 AA; 71094 MW; BCF91CFC304B4FEC CRC64;
MSHAIQTADL DWQLVDGIDV PVSKQFGDVY FSKDNGLLET RHVFLNGNDL STRLAELKPF
EYFCVGETGF GTGLNILALW QLWQQVRPDN HSRLHAISVE KFPLSKADLI RALNAWPELK
PLADQLIYQY PLPIAGCHRL SFPEERFSLD LWLGDAHDVF PRMEKTTAVN AWFLDGFAPS
CNPDMWEENA LNNIVRLSDY GTTFSSFSVA GVLKRGLRNH GISISRPRGF GHKREMLKAI
WNLPESEDTS ETPEDTAQKK NSLNSELKYQ ARQIAIIGAG IAGLSSAWAF ANRGHQVTIF
ERKAPLSGGS GNPLALLNPK LAPIEQSAEH MMTQAWQYAL NHYVRFKAFR PFQVHQLAIK
KPEDLLALAD EYPAGILETP AQDQQPDTEY PALALKQSGG VYPHQLRDEI LQHPNIQYLQ
AEISRIEAEP RLEPFADDQS LGQFDHVIVC TALNTPQLIE GLPDLKPIRG QVSWVENNGQ
SLDPNIAYSY GGYCIQLDDK HLLLGASFCV NRDDTEVLKE DHEHNRELIH SVFPEYTQTL
AEISEWHGRA SVRAQSRDYF PLLGKLKQDK EIYSLAGLGS KGFLFAPLCS EILAAQILGE
ACPASINMIK KLDVRRFEKK VKAKKPYFKP KS
//
