MNMG_SYNFM
ID MNMG_SYNFM Reviewed; 642 AA.
AC A0LEF5;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, 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=Sfum_0104;
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) 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; CP000478; ABK15807.1; -; Genomic_DNA.
DR RefSeq; WP_011696980.1; NC_008554.1.
DR AlphaFoldDB; A0LEF5; -.
DR SMR; A0LEF5; -.
DR STRING; 335543.Sfum_0104; -.
DR EnsemblBacteria; ABK15807; ABK15807; Sfum_0104.
DR KEGG; sfu:Sfum_0104; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_7; -.
DR OMA; FRPGYAI; -.
DR OrthoDB; 146811at2; -.
DR Proteomes; UP000001784; 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.
PE 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; NAD; Reference proteome; tRNA processing.
FT CHAIN 1..642
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000345348"
FT BINDING 10..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 122
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 177
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 269..283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 366
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 642 AA; 70555 MW; 331E23E5CC423640 CRC64;
MNKYEVIVVG AGHAGCEAAL AAARMGCRTL VLSICLDTVA HMPCSPSVGG VGKGHLVREI
DALGGRMALI TDRTAIQFRL LNTKKGPAVW GTRTQNDKAR YRISMKHCLE SEPNLDLKQA
HVESLAVEGN RIVGVIDQLG VFFGADAVVL ATGTFLRGLV HIGTTSVEAG RAGELASYPL
ANQLQRLGFT LGRMKTGTPA RLGRRSIDFS RFREQHGDEA PKPFSLFTDS IALPQVSCFI
GKTHQRTHEL VRRHIHLSPL YNGTIRGVSA RYCPSLEDKV MRFPDKDFHQ IILEPEGLDT
EEVYASGTGN SLPYDIQLRL IHSVPGLEEA EVMRPAYAIE YDFVQPTQLK ATLGSKLVEG
LYMAGQINGT SGYEEAAGQG LWAGINAALK AQGRPPFILD RSEAYLAVMV DDLVTRGTNE
PYRIFTSRAE YRLLLREDNA DLRLLEKGCE LGLHSADAAK ELRERRGAIR NELERLRLTH
VRPSAQVNQT LAENHSPPLD APAPLDKLLK RPELNYSTVA ILSPPPEPLS SKVTEQVEVE
CKYEGYLKRQ EAEVAKFRQL EQAAIPEDLM YDDIPGLSNE LRQKLGAVRP LSLGQATRIP
GMTPAAVSVL MVHLRRRAQG GPFLAPVLDP GVNMHSQKKK LA