ID   MNMG_PROMS              Reviewed;         655 AA.
AC   A2BTQ6;
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=A9601_18841;
OS   Prochlorococcus marinus (strain AS9601).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=146891;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS9601;
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; CP000551; ABM71167.1; -; Genomic_DNA.
DR   RefSeq; WP_011819285.1; NC_008816.1.
DR   AlphaFoldDB; A2BTQ6; -.
DR   SMR; A2BTQ6; -.
DR   STRING; 146891.A9601_18841; -.
DR   PRIDE; A2BTQ6; -.
DR   EnsemblBacteria; ABM71167; ABM71167; A9601_18841.
DR   KEGG; pmb:A9601_18841; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_3; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000002590; 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..655
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_1000016639"
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   655 AA;  73589 MW;  A1134D897916B4A8 CRC64;
     MQDHNSTNES FDVIVIGGGH AGCEAAITTA KLGFSTALFT INLDRIAWQP CNPAVGGPAK
     SQLVHEVDAL GGIIGKLADE TAIQKRILNA SRGPAVWALR AQTDKREYSK KMIEILQNTD
     NLSLKEAMIT ELDIAKTEQI GLNSKKILKK RIKGVKTFFG SYYSARSVII TAGTFLEGRI
     WIGNKSMSAG RSGEQAAQGL TQNLHEIGIK TERLKTGTPA RVDKRSIIFD ELDVQPSTAV
     DKYFSFDPDI KNNMPQVSCH ITRTTTKTHQ LIRDNLHLTP IYGGFIDSKG PRYCPSIEDK
     IVKFANKESH QIFLEPEGIN TPEIYVQGFS TGLPENIQLE LLRTLPGLGE CKMLRPAYAV
     EYDYIPATQL QTSLETKEIE YLFSAGQING TTGYEEAAAQ GLVAGVNATR KLNKKDPIIF
     SRESSYIGTM INDLITKDLK EPYRVLTSRS EYRLTLRGDN ADRRLTPLGY QIGLINEKRW
     SAYQEKMNLL EEEKFRLNNT RLKNTDEISK KIELETGSKI KGSTTLKELL KRPNFHYSDL
     IKYNLNERNL GSSIQEGVEI DIKYEGYLKR QKNNIEQINR QSCKSLPQEI NYEKIETLSL
     EARENLNKIK PKNFGDASKI PGVSKADLTA LLVWLKIREI KKEKANIFVE KKLSS