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Database: UniProt
Entry: A0A1Y2SBA5_9GAMM
LinkDB: A0A1Y2SBA5_9GAMM
Original site: A0A1Y2SBA5_9GAMM 
ID   A0A1Y2SBA5_9GAMM        Unreviewed;       682 AA.
AC   A0A1Y2SBA5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   05-JUN-2019, entry version 12.
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=Xvie_01067 {ECO:0000313|EMBL:OTA17223.1}, Xvie_03008
GN   {ECO:0000313|EMBL:OTA15202.1};
OS   Xenorhabdus vietnamensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=351656 {ECO:0000313|EMBL:OTA15202.1, ECO:0000313|Proteomes:UP000194350};
RN   [1] {ECO:0000313|EMBL:OTA15202.1, ECO:0000313|Proteomes:UP000194350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22392 {ECO:0000313|EMBL:OTA15202.1,
RC   ECO:0000313|Proteomes:UP000194350};
RA   Tobias N.J., Wolff H., Djahanschiri B., Pidot S.J., Stinear T.P.,
RA   Ebersberger I., Bode H.B.;
RT   "Systematic genetic and metabolomic analysis of Xenorhabdus and
RT   Photorhabdus spp., highlights the requirements for a dual symbiotic
RT   and pathogenic life style.";
RL   Submitted (OCT-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
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:OTA15202.1}.
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DR   EMBL; MUBJ01000018; OTA15202.1; -; Genomic_DNA.
DR   EMBL; MUBJ01000004; OTA17223.1; -; Genomic_DNA.
DR   Proteomes; UP000194350; 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   InterPro; IPR017610; tRNA_S-uridine_synth_MnmC_C.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF05430; Methyltransf_30; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR03197; MnmC_Cterm; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000194350};
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, ECO:0000313|EMBL:OTA15202.1};
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   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, ECO:0000313|EMBL:OTA15202.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00423459}.
FT   DOMAIN      118    243       Methyltransf_30. {ECO:0000259|Pfam:
FT                                PF05430}.
FT   DOMAIN      269    644       DAO. {ECO:0000259|Pfam:PF01266}.
FT   REGION        1    245       tRNA (mnm(5)s(2)U34)-methyltransferase.
FT                                {ECO:0000256|HAMAP-Rule:MF_01102}.
FT   REGION      273    682       FAD-dependent cmnm(5)s(2)U34
FT                                oxidoreductase. {ECO:0000256|HAMAP-Rule:
FT                                MF_01102}.
SQ   SEQUENCE   682 AA;  76924 MW;  933DB63A30427B82 CRC64;
     MKNRTINSAT LSWNEQGTPI SEQFDDVYFS NQDGLEETLY VFLKGNHFPQ RFNTHSRSEC
     VIAETGFGTG LNFLTLCRSF SHFRQQHPEA ALKRLHYISF EKYPLKPDDL KTAHQRWPEL
     KEFSAQLCQQ WPLALAGCHR LILANGAITL DLWFGDVNDL LPKISSNLTG KVDAWFLDGF
     APSKNPQMWS EQLFAAMAKF CRPEGTFATF TSAGIVRRGL QEAGFNVTKI KGFGRKREML
     TGILSPLNDP TPLTDTPWFS RKAALHTDDI AIIGGGVASA LTALALLRRG AKVTLYCQDD
     QPAQNASGNQ QGAIYPLLNG NDDPLERFFT SAFTFARRQY EQLIDENVLF DYQWCGVSQL
     AYDEKSASKI SKMLRTAWPE EIALGMNRNQ LSHVSGLDVN YDGIHYPQGG WLYPAQLTQA
     VIKLAEQRGM QIYFNHKVTQ LIQSESGWQL QIEDKENLQC KNHNVVIIAN GHCLPQFEQT
     KKLPVTSVRG QVSHIPTTNS LRQLKSVLCY DGYMTPVNPH TQYHCIGASY QRNQLDTQYS
     SIEQQENRER LLKCFPDVDW TQEVDISEEK SRQGIRCVIR DHMPMVGNVP VFSELMDKYA
     NLSQQINANK VIEKSPCYSG LFVLGALGSR GLCSAPLSAE LLASQIFGEA LPLDDETLAA
     LHPNRFWVRK LLRGKTVKAE RP
//
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