MNMG_PSELT
ID MNMG_PSELT Reviewed; 605 AA.
AC A8F522;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG {ECO:0000255|HAMAP-Rule:MF_00129};
DE AltName: Full=Glucose-inhibited division protein A {ECO:0000255|HAMAP-Rule:MF_00129};
GN Name=mnmG {ECO:0000255|HAMAP-Rule:MF_00129};
GN Synonyms=gidA {ECO:0000255|HAMAP-Rule:MF_00129};
GN OrderedLocusNames=Tlet_0690;
OS Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS TMO) (Thermotoga lettingae).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Pseudothermotoga.
OX NCBI_TaxID=416591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga lettingae TMO.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NAD-binding protein involved in the addition of a
CC carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of
CC certain tRNAs, forming tRNA-cmnm(5)s(2)U34. {ECO:0000255|HAMAP-
CC Rule:MF_00129}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00129};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00129}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00129}.
CC -!- SIMILARITY: Belongs to the MnmG family. {ECO:0000255|HAMAP-
CC Rule:MF_00129}.
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DR EMBL; CP000812; ABV33256.1; -; Genomic_DNA.
DR AlphaFoldDB; A8F522; -.
DR SMR; A8F522; -.
DR STRING; 416591.Tlet_0690; -.
DR EnsemblBacteria; ABV33256; ABV33256; Tlet_0690.
DR KEGG; tle:Tlet_0690; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_0; -.
DR OMA; FRPGYAI; -.
DR Proteomes; UP000002016; 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:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR Gene3D; 1.10.150.570; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR HAMAP; MF_00129; MnmG_GidA; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR004416; MnmG.
DR InterPro; IPR002218; MnmG-rel.
DR InterPro; IPR020595; MnmG-rel_CS.
DR InterPro; IPR026904; MnmG_C.
DR InterPro; IPR044920; MnmG_C_subdom.
DR InterPro; IPR040131; MnmG_N.
DR PANTHER; PTHR11806; PTHR11806; 1.
DR PANTHER; PTHR11806:SF0; PTHR11806:SF0; 1.
DR Pfam; PF01134; GIDA; 1.
DR Pfam; PF13932; GIDA_C; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR00136; gidA; 1.
DR PROSITE; PS01280; GIDA_1; 1.
DR PROSITE; PS01281; GIDA_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; NAD; Reference proteome; tRNA processing.
FT CHAIN 1..605
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000345352"
FT BINDING 107
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 162
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 257..271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 354
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 605 AA; 68315 MW; AB952B9E9ABFED62 CRC64;
MEAALATARL GFKTALLTSN LDRVAWAPCN PAIGGPAKGI IVREIDALGG EMAKVTDETM
INVRMLNTSK GASVRALRAQ IDKVSYSQKM KRILEETQNL YLRHSQVCDI LVEKGKVKSV
VDTLGIEYKS RAIILTAGTF LNGKIFIGHA TFEAGRLGDF PSKGLTESLE KYGIRFQRFK
TGTPARILGK SIDFSKMIRQ DTSKEPLCFS YFDKPVILSK DYPCWLTYTN EKTHEIIRKN
LRFSPLYGDV KLIVGKGPRY CPSIEDKVVK FPSKNMHQIF VEPEGKTTGE YYLNGLSTSL
PYEVQLEMIR TIPGLENAHI TRPAYAIEYD YADPTQLYHT LESKIVEGLF LAGQINGTSG
YEEAAGQGLI AGINAALKLR GENQFTLDRS EAYIGVMIDD IVTKGVDEPY RILTSRAEFR
LLLRHDNAHL RLSKKGYQIG LIPKWFYEEI LTLESRIKTE IERLKQVSIK PTGQINDFLT
SINTHPLRQP TTLFQILKRP DITYEQLRSL DPSPMDSPEV IEQIELTAKY EDYIEKMLEE
TKVFNDLEKI TIPEAIDYGK IPNLSVVARE KLEKIRLRNV LQVSRVPGIT PADILALITY
LKSFK