ID   MNMG_PROM5              Reviewed;         654 AA.
AC   A2BZ61;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=P9515_18651;
OS   Prochlorococcus marinus (strain MIT 9515).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167542;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9515;
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; CP000552; ABM73072.1; -; Genomic_DNA.
DR   RefSeq; WP_011821156.1; NC_008817.1.
DR   AlphaFoldDB; A2BZ61; -.
DR   SMR; A2BZ61; -.
DR   STRING; 167542.P9515_18651; -.
DR   PRIDE; A2BZ61; -.
DR   EnsemblBacteria; ABM73072; ABM73072; P9515_18651.
DR   KEGG; pmc:P9515_18651; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_3; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000001589; 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..654
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_1000016638"
FT   BINDING         17..22
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         289..303
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   654 AA;  73176 MW;  2FEB638C74A75AFB CRC64;
     MKKQQSSNES FDVIVIGGGH AGCEAAITTA KLGFSTALFT INLDRIAWQP CNPAVGGPAK
     SQLVHEVDAL GGIIGKLADE TAIQKRILNA SRGPAVWALR AQTDKREYSK RMIEILQNTD
     NLSLKEAMIT ELLIKEVETF TKNSKNTTKQ IKGVKTFFGT CYSAKSIIIT AGTFLEGRIW
     IGNKSMSAGR SGEQAAQGLT ESLHSLGIKT ERLKTGTPAR VDKKSISFDA LDIQPSTASD
     KYFSFDPKIK NDMPQICCHI TRTTQKTHEL IRNNLHLTPI YGGFIDSKGP RYCPSIEDKI
     VKFADKNSHQ IFLEPEGINT PEIYVQGFST GLPENIQLEL LRTLPGLNKC KMLRPAYAVE
     YEYIPATQLK LSLETIEIDN LFSAGQINGT TGYEEAAAQG LVAGINATRK LNMKDPIIFS
     RESSYIGTMI NDLITRDLKE PYRVLTSRSE YRLTLRGDNA DRRLTPLGFE IGLIDERRWF
     AHKEKMKLLK EENSRLENTR LKCTDEIARN IELESGSKIK GSTTLKDLLK RPNVHYSDFI
     KYDLANKSLP IAVMEGVEID IKYEGYLKRQ QNNIDQINRQ SLKSLPIEIN YDLIDTLSLE
     ARENLNKIKP TNFGDASKIP GVSKADLTAL LVWLKIKEIK KEKTNSFVEK KLSS