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Database: UniProt
Entry: A0A0Q7T549_9CAUL
LinkDB: A0A0Q7T549_9CAUL
Original site: A0A0Q7T549_9CAUL 
ID   A0A0Q7T549_9CAUL        Unreviewed;       604 AA.
AC   A0A0Q7T549;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   03-JUL-2019, entry version 27.
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=ASD25_20505 {ECO:0000313|EMBL:KQY90890.1};
OS   Brevundimonas sp. Root1423.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=1736462 {ECO:0000313|EMBL:KQY90890.1, ECO:0000313|Proteomes:UP000051815};
RN   [1] {ECO:0000313|Proteomes:UP000051815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1423 {ECO:0000313|Proteomes:UP000051815};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQY90890.1, ECO:0000313|Proteomes:UP000051815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1423 {ECO:0000313|EMBL:KQY90890.1,
RC   ECO:0000313|Proteomes:UP000051815};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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
CC       position (U34) in tRNA. Catalyzes the FAD-dependent demodification
CC       of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a
CC       methyl 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       ECO:0000256|SAAS:SAAS00015108}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-
CC         methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA +
CC         H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19569,
CC         Rhea:RHEA-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, ECO:0000256|SAAS:SAAS01118306};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01102, ECO:0000256|SAAS:SAAS00179145};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01102,
CC       ECO:0000256|SAAS:SAAS00015101}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the DAO family.
CC       {ECO:0000256|HAMAP-Rule:MF_01102, ECO:0000256|SAAS:SAAS00540894}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       methyltransferase superfamily. tRNA (mnm(5)s(2)U34)-
CC       methyltransferase family. {ECO:0000256|HAMAP-Rule:MF_01102,
CC       ECO:0000256|SAAS:SAAS00540888}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KQY90890.1}.
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DR   EMBL; LMFL01000010; KQY90890.1; -; Genomic_DNA.
DR   EnsemblBacteria; KQY90890; KQY90890; ASD25_20505.
DR   Proteomes; UP000051815; 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)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0002097; P:tRNA wobble base modification; IEA:UniProtKB-UniRule.
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; IPR023032; tRNA_MAMT_biosynth_bifunc_MnmC.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF05430; Methyltransf_30; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000051815};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00423465};
KW   FAD {ECO:0000256|HAMAP-Rule:MF_01102, ECO:0000256|SAAS:SAAS00015112};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00423462};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00015105};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00423464};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00015110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051815};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00423457};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00423476};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00423459}.
FT   DOMAIN      110    231       Methyltransf_30. {ECO:0000259|Pfam:
FT                                PF05430}.
FT   DOMAIN      244    568       DAO. {ECO:0000259|Pfam:PF01266}.
FT   REGION        1    232       tRNA (mnm(5)s(2)U34)-methyltransferase.
FT                                {ECO:0000256|HAMAP-Rule:MF_01102}.
FT   REGION      247    604       FAD-dependent cmnm(5)s(2)U34
FT                                oxidoreductase. {ECO:0000256|HAMAP-Rule:
FT                                MF_01102}.
SQ   SEQUENCE   604 AA;  62200 MW;  8A47343DFC0518F7 CRC64;
     MADDRSPRLI WTEDGALRSG RFDDVYFSQQ DGLAETRAVF LTGCGLPEAW SGRRRFTVAE
     LGFGTGLNIA ALLDLWRREG PPDGRLHVFS VEGFPLGREE AARALSAWPE LAGASEALLA
     AWPAPTPGFH RLDLPGFNAV VDLAIGDVAW ALEQWAGRAD AWFLDGFAPS TNPGMWSDAV
     MDGIAARSAP GARAATFTVA GSVRRGLAGR GFAVAKRPGH GRKRERLEAW LPGAANEAAA
     GPSVAVVGAG IAGASMARAF AALGVRPVVY EADRPGAGAS GFPAALVTPR LDAGDAGIAA
     LFAQALDRAR ALYAAAPGAV LDRGVLQLEQ QARDAGRFGK VAEQPVWPEG GMAVLDAAAC
     SARLGEPVDG GLLMGEALAL QPAPVLAQWL TQADRATAEV AGVEPHDGGW RLIAGDGEII
     AEADIVVVAA GWGVAGLWPE APLSPVRGQA DWVEGVVAPP VAWGGYAVPT GEGLLFGATH
     DRGEVGKEIR RADSERNLAV LAARLPGLAA RVEAAGPGQA RAAVRATTPD RLPLAGPVSG
     RPGLFVLGGL GSRGFCAAPL LAEHVAALAL GAPSPLPADL AARVDPARWR KTGSLAHLVD
     KAEG
//
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