ID   MNMG_PROM3              Reviewed;         653 AA.
AC   A2CDR8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=P9303_28981;
OS   Prochlorococcus marinus (strain MIT 9303).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9303;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(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; CP000554; ABM79628.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2CDR8; -.
DR   SMR; A2CDR8; -.
DR   STRING; 59922.P9303_28981; -.
DR   EnsemblBacteria; ABM79628; ABM79628; P9303_28981.
DR   KEGG; pmf:P9303_28981; -.
DR   HOGENOM; CLU_007831_2_2_3; -.
DR   OMA; FRPGYAI; -.
DR   BioCyc; PMAR59922:G1G80-2541-MON; -.
DR   Proteomes; UP000002274; 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; tRNA processing.
FT   CHAIN           1..653
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_1000016637"
FT   BINDING         17..22
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         293..307
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   653 AA;  71487 MW;  AA87020B52078F09 CRC64;
     MPFSAPPTEH FDVIVVGGGH AGCEAALTAA RLGLSTALFT LNLDRIAWQP CNPAVGGPAK
     SQLVHEVDAL GGVIGRLADA TALQKRVLNA SRGPAVWALR AQTDKRLYSR QMLQLLQQTA
     NLSLREAMVT GLEVKGDPSG GGEHWEPAQG HAAQITGVRT YFGSIYRAQA VVLTTGTFLG
     GQIWVGNQSM PAGRAGEQAA EGLTEALESL GFQTNRLKTG TPARVDRRSI ALDQLEEQPS
     DAADRFFSFD PTTWVSGEQM SCHITRTTAS THQLIKENLE LTPIYGGFLD SKGPRYCPSI
     EDKIVRFADK DSHQIFLEPE GRDTPEIYVQ GFSTGLPERL QLDLLRTLPG LEQCIMLRPA
     YAVDYDYLPA TQLSPSLQTK RVKGLFTAGQ LNGTTGYEEA AAQGLVAGLN AARLVHGQEQ
     VHFPREGSYI GTMIDDLVSK DLHEPYRVLT SRSEYRLILR GDNADRRLTP LGYQLGLIDA
     RRWQLFQSKQ TALEDEKQRL EKQRIKASDP AAPALEAKTG AKIKGSITLA DLLRRPGVHS
     ADLIEHGLVD PELALGVREG AEIDIKYSGY LQRQQQQIDQ LKRQSQRRLP ANLDYANIST
     LSKEAREKLT AVGPLNFAQA SQIPGVSKAD LTALLVWLEL QKRRTLAASG HDR