ID   MNMG_MYCAP              Reviewed;         613 AA.
AC   A5IXW3;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-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}; OrderedLocusNames=MAG1740;
OS   Mycoplasmopsis agalactiae (strain NCTC 10123 / CIP 59.7 / PG2) (Mycoplasma
OS   agalactiae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=347257;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10123 / CIP 59.7 / PG2;
RX   PubMed=17511520; DOI=10.1371/journal.pgen.0030075;
RA   Sirand-Pugnet P., Lartigue C., Marenda M., Jacob D., Barre A., Barbe V.,
RA   Schenowitz C., Mangenot S., Couloux A., Segurens B., de Daruvar A.,
RA   Blanchard A., Citti C.;
RT   "Being pathogenic, plastic, and sexual while living with a nearly minimal
RT   bacterial genome.";
RL   PLoS Genet. 3:744-758(2007).
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; CU179680; CAL58872.1; -; Genomic_DNA.
DR   RefSeq; WP_011949354.1; NC_009497.1.
DR   AlphaFoldDB; A5IXW3; -.
DR   SMR; A5IXW3; -.
DR   STRING; 347257.MAG1740; -.
DR   PRIDE; A5IXW3; -.
DR   EnsemblBacteria; CAL58872; CAL58872; MAG1740.
DR   KEGG; maa:MAG1740; -.
DR   HOGENOM; CLU_007831_2_2_14; -.
DR   OMA; FRPGYAI; -.
DR   Proteomes; UP000007065; 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..613
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345302"
FT   BINDING         11..16
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         271..285
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   613 AA;  68450 MW;  4DAFC604A3AADD0A CRC64;
     MNKKYDAIVI GGGHAGLEAA FAISHKGRNT LLLTFNSKKL GMMPCNPSIG GPAKGIITRE
     IDALGGMQGL WADLATIQLK MLNLSKGPAV RALRAQIDKE KYSQLAYEYV LKQPNLELLE
     GVAEEVIVDE NGYFKGVLVE NIGLIEAKVC VITTGTYMNS RILRGQDITT SGPDNEKTTP
     KLSASLAKLG FTLQRLKTGT PPRIYSDSIN FDEVEQEVLS DVNISFSSRS NLKKPKQIAC
     YLTYTTPETH RIIEENIHRS PMYSGVIEGI GPRYCPSVED KIVKFPDKER HQIFFEPETA
     DGAITHVNGL STSMPIDVQE LMIKSIPGLR NAKVQKWAYA IEYDALDPLQ LKESLETKLV
     HNLFTAGQIN GTSGYEEAAA QGLIAGINAA LKLEDKDPIV ILRNHGYIGV LIDDLVTKGT
     KEPYRMLTSR AEYRLLLRND NADDRLSEYA YNSGMISKEE YQKVLDKYKL IDDEIQRLNT
     TYLSGKSDVA LKYNITNGST LLNVISRPDV DPSDIIPNFP YLEEITTMVR LHGYIEKQKS
     DANKAVRLEN LKIPEDLNYL DVKNIAIEAR QKFEKIRPAT IGQASRISGI NPADIQMLMF
     HLESRNKKNY DQN