ID   MNMG_ALBFT              Reviewed;         679 AA.
AC   Q21QL5;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Rfer_0049;
OS   Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS   (Rhodoferax ferrireducens).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL   Submitted (FEB-2006) 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; CP000267; ABD67811.1; -; Genomic_DNA.
DR   RefSeq; WP_011462384.1; NC_007908.1.
DR   AlphaFoldDB; Q21QL5; -.
DR   SMR; Q21QL5; -.
DR   STRING; 338969.Rfer_0049; -.
DR   EnsemblBacteria; ABD67811; ABD67811; Rfer_0049.
DR   KEGG; rfr:Rfer_0049; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_4; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000008332; 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..679
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345325"
FT   BINDING         13..18
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         280..294
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   679 AA;  74275 MW;  654E75F09F006A27 CRC64;
     MLYPQHFDVI VVGGGHAGTE AALAAARMGC KTLLLSHNIE TLGQMSCNPS IGGIGKGHLV
     KEVDALGGAM AAATDEGGIQ FRILNSSKGP AVRATRAQAD RLLYKAAIRR RLENQPNLWL
     FQQAVDDLMV EGDRVVGAVT QAGIKFRAKT VVLTAGTFLD GKIHVGLNNY AAGRAGDPPA
     VRLSARLKEL KLPQGRLKTG TPPRLDGRSI DFSKCGEQPG DGMPGGMSPV MPVFSFMGRV
     EQHPPQMSCW TTHTNERTHE IIRSGFDRSP MFTGKIEGVG PRYCPSVEDK INRFADKDSH
     QIFLEPEGLT TNEYYPNGIS TSLPFDIQYA LVRSMAGLEN AHILRPGYAI EYDYFDPQQL
     KSSFETRAIG GLFFAGQING TTGYEEAAAQ GLFAGVNAAL QAGAQTSWQQ ETWVPGRDEA
     YLGVLVDDLI TKGVTEPYRM FTSRAEFRLQ LREDNADMRL TETGRRLGLV DDARWEAFSR
     KREAVSRETE RLRSLWVSPK NLTATESERV LGKSIEHEYS LADLLRRPDV NYANLMSLEG
     GKYASAELNI PVSRETPAVP LPEAVFAAVV IEQVEIVAKY AGYIDRQIEE VGRAAHYENL
     KLPLELDYLQ VSALSFEARQ KLSKHRPETL GQASRLSGIT PAAISLLLVH LKKSNFKGFA
     AAGKVTAPSE SGDVQQGVI