MNMG_SYNAS
ID MNMG_SYNAS Reviewed; 639 AA.
AC Q2LXU8;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 81.
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=SYNAS_30300; ORFNames=SYN_01650;
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB;
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABC78909.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000252; ABC78909.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041585804.1; NC_007759.1.
DR AlphaFoldDB; Q2LXU8; -.
DR SMR; Q2LXU8; -.
DR STRING; 56780.SYN_01650; -.
DR PRIDE; Q2LXU8; -.
DR EnsemblBacteria; ABC78909; ABC78909; SYN_01650.
DR KEGG; sat:SYN_01650; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_7; -.
DR OrthoDB; 146811at2; -.
DR Proteomes; UP000001933; 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..639
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000345349"
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 639 AA; 70796 MW; 7F6EBBC665805F5E CRC64;
MRQFDVIVVG AGHAGCEAAL AASRMGCETL LFNINLDSIA LMSCNPAIGG LAKGQLVKEI
DALGGEMGRM ADKTAVHFRI LNASKGPAVQ SSRVQCDKQL YRLAMKSVVE RQPKLHLFQS
LVDCLLVKDG QITGVADQTG VCFGAKAVVI TTGTFLNGLV HVGTSHYPAG RAGEIASISL
ANCLRKMGFE MGRMKTGTPP RLKASTIDFS RLERQDSDPA FEPFSLSTER LGKERLPSYF
GYTTSETHRL IRDNIRFSPL YSGVIKGVSA RYCPSLEDKV MRFADKGRHP VVLEFEGLET
EEVYAKGLGN SLPLDLQEQI VHSVPGLENS EILRSAYAIE YDFVQPTQLN HTLETKRVRG
LYLAGQINGT SGYEEAAAQG MWAGINAALA VQGRPPFVLD RSEAYMGVLI DDLVTQGVDE
PYRMFTSRAE YRLILREDNA ALRLTPRGFD LGLIPQDLHE QISERIRRIE EGMKCLSSFK
IYPGTAVNSK LEEHGSPAIK NPVTLFQLLK RTDLSWEDLS MFQDLPDFPE DVPDGYDRMI
RKQIEIEAKY EGYIQRQREA VVRMKALESR RIPPGMDYSA IPGLSNELRM KLARVEPETI
GQARRITGMT QAALAAVMIM IKKKEQDTRG QSPLPAQSE
