ID E1V8E2_HALED Unreviewed; 674 AA.
AC E1V8E2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 78.
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:CBV43598.1};
GN OrderedLocusNames=HELO_3714 {ECO:0000313|EMBL:CBV43598.1};
OS Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS / 1H9).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=768066 {ECO:0000313|EMBL:CBV43598.1, ECO:0000313|Proteomes:UP000008707};
RN [1] {ECO:0000313|Proteomes:UP000008707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9
RC {ECO:0000313|Proteomes:UP000008707};
RX PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA Kunte H.J.;
RT "A blueprint of ectoine metabolism from the genome of the industrial
RT producer Halomonas elongata DSM 2581(T).";
RL Environ. Microbiol. 13:1973-1994(2011).
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}.
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DR EMBL; FN869568; CBV43598.1; -; Genomic_DNA.
DR AlphaFoldDB; E1V8E2; -.
DR STRING; 768066.HELO_3714; -.
DR KEGG; hel:HELO_3714; -.
DR eggNOG; COG0665; Bacteria.
DR eggNOG; COG4121; Bacteria.
DR HOGENOM; CLU_022427_1_0_6; -.
DR OrthoDB; 9786494at2; -.
DR Proteomes; UP000008707; 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)(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};
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 128..246
FT /note="MnmC-like methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF05430"
FT DOMAIN 272..643
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT REGION 1..248
FT /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01102"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..674
FT /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01102"
FT COMPBIAS 18..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 674 AA; 72794 MW; 387E8F037EAE9422 CRC64;
MPPAHDPLPP LAGLTRAHLD WRPDDGGEDT PHSSEFDDVY FSRHDGRAET EHVFLDANRL
PERFQDWTED RPFVIGETGF GTGLNMLCAW ACFDAHAPAR ARLHLVSTEL YPLDRRDLAR
ALAAWPDLAD RAAVLLAQWP EPVSGVHRLW LDARVTLDLH FGDTAERLRW LDGRVDAWFL
DGFAPARNPD MWQPALFAAM AARSRPGATF ATFTCAGVVK RGLAAAGFAW RKVPGFGRKR
EMLAGEIATP PADERRRATP WFTPPAPCPR RRVAVIGGGI AGTSVAAALA RRGVAVTLID
REGPGAGASG NRQGVLYVKL AAETNDQSRC YLAGLLHSRR WLDALDPDGS LWQPCGVLQL
ATTPREAKRQ TAFLANHPLP DSVVRGVSSE QASQLADIPI ENGGLEYPLA GWVRPDALCR
RLAATPGVTL LRAEVDDITA TPEGWRLSMT TDQGPDEFDA DQVVIATASL ANRFTQTADL
PLQPVRGQVS SLTLPENAPA PSRVICAGGY VAPPREGRLT FGATFRPNET DTRVSDADHR
ANRDELTRTL PGYAAALEGS GAPLDTAAFD GRAAVRAASP DKTPYAGPVP DAAAWRQAYA
LLAKDATRIP DLAGQHHPGL WISAAHGSRG LASAPLCAEV IASRICDEPM PLEAPLVDHL
HPGRRLIREL IRGG
//
