ID   MNMG_PROM0              Reviewed;         660 AA.
AC   A3PFG3;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-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=P9301_18651;
OS   Prochlorococcus marinus (strain MIT 9301).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9301;
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; CP000576; ABO18488.1; -; Genomic_DNA.
DR   RefSeq; WP_011863770.1; NC_009091.1.
DR   AlphaFoldDB; A3PFG3; -.
DR   SMR; A3PFG3; -.
DR   STRING; 167546.P9301_18651; -.
DR   PRIDE; A3PFG3; -.
DR   EnsemblBacteria; ABO18488; ABO18488; P9301_18651.
DR   KEGG; pmg:P9301_18651; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_3; -.
DR   OMA; FRPGYAI; -.
DR   Proteomes; UP000001430; 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..660
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345317"
FT   BINDING         17..22
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         290..304
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   660 AA;  74300 MW;  E87EE511C8D679E8 CRC64;
     MQDHHSTNES FDVIVIGGGH AGCEAAITTA KLGFSTALFT INLDRIAWQP CNPAVGGPAK
     SQLVHEVDAL GGIIGKLADE TAIQKRILNA SRGPAVWALR AQTDKREYSK KMIEILQNTD
     NLSLKEAMIT ELDIAKTEEI GLNSKRTVKK RIKGVRTFFG SYYSARSVII TAGTFLEGRI
     WIGNKSMSAG RSGEQAAKGL TENLHEIGIK TERLKTGTPA RVDKRSIIFD DLDIQPSTAA
     DKYFSFDPDI KNNMPQVSCH ITRTTTKTHQ LIRDNLHLTP IYGGFIDSKG PRYCPSIEDK
     IVKFADKESH QIFLEPEGIN TPEIYVQGFS TGLPENIQLE LLRTLPGLNE CKMLRPAYAV
     EYDYIPATQL QTSLETKEIE YLFSAGQING TTGYEEAAAQ GLVAGVNATR KLSKKDPIIF
     TRESSYIGTM INDLITKDLK EPYRVLTSRS EYRLTLRGDN ADRRLTQLGY QIGLINEKRW
     SAYQEKMKLL EEEKFRLNKT RLKNTEEISK KIELETGSKI KGSITLKELL KRPDFHYSDL
     IKYNLTEKNL GSSIQEGVEI DIKYEGYLKR QKNNIEQINR QSCKSLPQEI NYEKIETLSL
     EARENLNKIK PKNFGDASKI PGVSKADLTA LLVWLKIREI KKEKANIFIE KKLSSKKHSV