ID   MNMG_RHOPA              Reviewed;         622 AA.
AC   Q6ND15;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 2.
DT   03-AUG-2022, entry version 100.
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}; OrderedLocusNames=RPA0294;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAE25738.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX572593; CAE25738.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_042440689.1; NC_005296.1.
DR   AlphaFoldDB; Q6ND15; -.
DR   SMR; Q6ND15; -.
DR   STRING; 258594.RPA0294; -.
DR   PRIDE; Q6ND15; -.
DR   EnsemblBacteria; CAE25738; CAE25738; RPA0294.
DR   GeneID; 66891304; -.
DR   KEGG; rpa:RPA0294; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_5; -.
DR   PhylomeDB; Q6ND15; -.
DR   BioCyc; RPAL258594:TX73_RS01525-MON; -.
DR   Proteomes; UP000001426; 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..622
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000117163"
FT   BINDING         11..16
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         270..284
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   622 AA;  67063 MW;  FE300A01903D5782 CRC64;
     MRTSFDVIVI GGGHAGCEAA AAAARIGAAT ALVTHRFATV GAMSCNPAIG GLGKGHLVRE
     VDALDGLMGR VADAGGIQFR MLNRRKGPAV RGPRAQADRK LYAAAMQTAI QGFPNLSVIE
     GEADALLWQD GRVSGIRLGD GREFAAAAVV ITTGTFLRGL IHLGERSWPA GRIDEAPAMG
     LSSSFEALGF KLGRLKTGTP PRLDGRTIDW SAVEMQPGDD PAEPFSVLTP AITTPQIECG
     ITRTTTATHE VIRANVHRSP MYSGQIQSTG PRYCPSIEDK IVKFGDRDGH QIFLEPEGLD
     DPTVYPNGIS TSLPEEVQRA ILKTIPGLER TEMLRPGYAI EYDHVDPREL EPTLQTKRLR
     GLFLAGQING TTGYEEAAAQ GLVAGLNAGL SAGGGDLVVF DRADGYLGVM IDDLVTRGIT
     EPYRMFTSRA EYRLTLRADN ADQRLTDKGL ALGCVGVERS AFHHDKMSAL SDAKALAQSL
     SITPNEAAKH GLALNRDGQR RSAFDLLSYP EIEWAQVRAI WPELGKVDPA IAVHVEIDAK
     YHVYLERQTA DVEAFRRDES LGLTDVDYAA VPGLSNEART RLERHRPHTV GQAGRLDGIT
     PAALGILAAY LRREQRKRKS TG