MNMG_NITMU
ID MNMG_NITMU Reviewed; 632 AA.
AC Q2Y5B4;
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=Nmul_A2770;
OS Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=323848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25196 / NCIMB 11849 / C 71;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT 25196.";
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB76057.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000103; ABB76057.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011382042.1; NZ_FNVK01000022.1.
DR AlphaFoldDB; Q2Y5B4; -.
DR SMR; Q2Y5B4; -.
DR STRING; 323848.Nmul_A2770; -.
DR EnsemblBacteria; ABB76057; ABB76057; Nmul_A2770.
DR KEGG; nmu:Nmul_A2770; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_4; -.
DR OrthoDB; 146811at2; -.
DR Proteomes; UP000002718; 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..632
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000345309"
FT BINDING 13..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 180
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 273..287
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 370
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 632 AA; 69163 MW; 495BC364C0FA5593 CRC64;
MTVPEIFDVI VIGGGHAGTE AALAAARIGQ KTLLLSHNIE TLGQMSCNPS IGGIGKGHLV
KEIDALGGVM AEAADEAGIQ FRILNSRKGP AVRATRAQAD RVLYRQAIRQ RLESQPNLWL
FQQGVDDLVL EGERVAGVVT QLGIRFNARA VILTAGTFLA GLAHVGSANF QAGRAGDLPS
NSLAGRLREL KLPVGRLKTG TPPRIDGRTI DYSAVAAQPG DAPVPVFSFM GNAASHPKQV
SCWITHTNSQ THDIIRSGLD RSPLFSGAIE GIGPRYCPSI EDKVVRFSAK ESHQIFLEPE
GLTTHEVYPN GISTSLPFDM QVKLVRSIKG LENAHITRPG YAIEYDYFDP RALKSSLETR
MIEGLFFAGQ INGTTGYEEA AAQGLLAGIN AALKTQDREP WCPRRDEAYL GVLVDDLITR
GVTEPYRMFT SRAEYRLQLR EDNADLRLTE VGRRLGVVND ARWVAFNIKL EAIAQEQNRL
KTTWLSPKSL SETDALRVIG KNIEHECSLH DLLRRPNVSY AELMTLPGAG EPVVDLAAAE
QVEIQAKYQG YIERQKDEVA RNAYYEDIRL PQDLDYKTVR GLSNEVQQKL NQFKPETAGQ
ASRISGITPA AISLLLVHVK RGFSSANTKK SA