ID MNMG_VARPS Reviewed; 652 AA.
AC C5CW10;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
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=Vapar_0045;
OS Variovorax paradoxus (strain S110).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=543728;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S110;
RX PubMed=21183664; DOI=10.1128/jb.00925-10;
RA Han J.I., Choi H.K., Lee S.W., Orwin P.M., Kim J., Laroe S.L., Kim T.G.,
RA O'Neil J., Leadbetter J.R., Lee S.Y., Hur C.G., Spain J.C.,
RA Ovchinnikova G., Goodwin L., Han C.;
RT "Complete genome sequence of the metabolically versatile plant growth-
RT promoting endophyte, Variovorax paradoxus S110.";
RL J. Bacteriol. 193:1183-1190(2011).
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; CP001635; ACS16708.1; -; Genomic_DNA.
DR AlphaFoldDB; C5CW10; -.
DR SMR; C5CW10; -.
DR STRING; 543728.Vapar_0045; -.
DR KEGG; vap:Vapar_0045; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_4; -.
DR OrthoDB; 9815560at2; -.
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; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.150.570; GidA associated domain, C-terminal subdomain; 1.
DR Gene3D; 1.10.10.1800; tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG/GidA; 1.
DR HAMAP; MF_00129; MnmG_GidA; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR049312; GIDA_C_N.
DR InterPro; IPR004416; MnmG.
DR InterPro; IPR002218; MnmG-rel.
DR InterPro; IPR020595; MnmG-rel_CS.
DR InterPro; IPR026904; MnmG_C.
DR InterPro; IPR047001; MnmG_C_subdom.
DR InterPro; IPR044920; MnmG_C_subdom_sf.
DR InterPro; IPR040131; MnmG_N.
DR NCBIfam; TIGR00136; gidA; 1.
DR PANTHER; PTHR11806; GLUCOSE INHIBITED DIVISION PROTEIN A; 1.
DR PANTHER; PTHR11806:SF0; PROTEIN MTO1 HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF01134; GIDA; 1.
DR Pfam; PF13932; GIDA_C; 1.
DR Pfam; PF21680; GIDA_C_1st; 1.
DR SMART; SM01228; GIDA_assoc_3; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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..652
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_1000203171"
FT BINDING 13..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 279..293
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 652 AA; 71818 MW; BDA926E187495608 CRC64;
MLYPEEFDVI VVGGGHAGTE AALAAARMGA KTLLLSHNIE TLGQMSCNPS IGGIGKGHLV
KEVDALGGAM AIATDEAGIQ FRILNSSKGP AVRATRAQAD RVLYKAAIRH RLENQPNLSL
FQQAVDDLMV EGDRVVGAVT QVGIAFRART VVLTAGTFLD GRIHVGLDNY QAGRAGDPPA
VSLSARLKEL KLPQGRLKTG TPPRLDGRSI DFSKCTEQAG DGMPGGAGPM PVFSFMGRAD
MHPQQMPCWI THTNARTHDI IRSGFDRSPM FTGKIDGVGP RYCPSVEDKI NRFADKESHQ
IFLEPEGLTT NEYYPNGIST SLPFDIQYQL VRSMPGLENA HILRPGYAIE YDYFDPRELK
SSFETRSIKG LFFAGQINGT TGYEEAAAQG LFAGINAALQ CRGEEAWLPR RDEAYLGVLV
DDLITKGVTE PYRMFTSRAE FRLQLREDNA DMRLTEAGRK LGLVDDARWD AFSRKRDTVS
RETERLKSIW VNPRNLPAAE SERVLGKAIE HEYNLADLLR RPDVNYETLM SLDGGKYSAG
SPLSEIEIEQ IEISAKYSGY IERQHDEVER AAHFENLRLP ADFDYSQVKA LSFEVRQKLD
KHRPETLGLA SRISGVTPAA ISLLMIHLRK GGHKAFNRDA ATEAAAESQP AQ
//
