MNMG_SYNS9
ID MNMG_SYNS9 Reviewed; 641 AA.
AC Q3AUG9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=Syncc9902_2197;
OS Synechococcus sp. (strain CC9902).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=316279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9902;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9902.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000097; ABB27155.1; -; Genomic_DNA.
DR RefSeq; WP_011360933.1; NC_007513.1.
DR AlphaFoldDB; Q3AUG9; -.
DR SMR; Q3AUG9; -.
DR STRING; 316279.Syncc9902_2197; -.
DR PRIDE; Q3AUG9; -.
DR EnsemblBacteria; ABB27155; ABB27155; Syncc9902_2197.
DR KEGG; sye:Syncc9902_2197; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_3; -.
DR OMA; FRPGYAI; -.
DR OrthoDB; 146811at2; -.
DR Proteomes; UP000002712; 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..641
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_1000016702"
FT BINDING 17..22
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 281..295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 641 AA; 70402 MW; C341781866E45C4E CRC64;
MSFTAAPTES FDVIVVGGGH AGCEAAITTA RLGLNTALFS LNLDRIAWQP CNPAVGGPAK
SQLVHEVDAL GGVIGRLADA TAIQKRTLNA SRGPAVWALR AQTDKRLYSR QMLQLLQHTP
NLALREAMVT GLEVEGEEEQ QRIQGVRTYF GSVYAAQAVV LTAGTFLGGR IWVGHQSMAA
GRAGEQAAEG LTETLQGLGF HTDRLKTGTP ARVDRRSIAL DQLEEQPSDA ADRFFSFDPA
AWVSGEQMSC HITRTTAETH QLIRDNLHLT AIYGGVIDSK GPRYCPSIED KIVRFADKES
HQIFLEPEGR DTPEIYVQGF STGLPEPIQL QLLRSLPGLE QAVMLRPAYS VDYDYLPATQ
LKPSLETKRV SGLFSAGQLN GTTGYEEAAA QGLVAGLNAA RLIGEQDPVY FPREGSYIGT
MIDDLVSQDL REPYRVLTSR SEYRLILRGD NADRRLTPLG RDLGLIDDRR WQLFEEKLQA
MDAEKKRLES TRLKVSDPIA PTVEEETGAP IKGSITLADL LRRPAMHAAD LVRHGLADGD
LPLPVREGAE IDIKYSGYLQ RQQQQIDQVK RQSQRKLPSD LNYTNIGTLS NEAREKLSAI
QPTTLGQANR IPGVSQADIT ALLMWLELQK RQPLAPTTQA R