MNMG2_CALS4
ID MNMG2_CALS4 Reviewed; 633 AA.
AC Q8R6K9;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG 2 {ECO:0000255|HAMAP-Rule:MF_00129};
DE AltName: Full=Glucose-inhibited division protein A 2 {ECO:0000255|HAMAP-Rule:MF_00129};
GN Name=mnmG2 {ECO:0000255|HAMAP-Rule:MF_00129};
GN Synonyms=gidA2 {ECO:0000255|HAMAP-Rule:MF_00129};
GN OrderedLocusNames=TTE2795;
OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobacter.
OX NCBI_TaxID=273068;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX PubMed=11997336; DOI=10.1101/gr.219302;
RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA Wang J., Yu J., Yang H.;
RT "A complete sequence of the T. tengcongensis genome.";
RL Genome Res. 12:689-700(2002).
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; AE008691; AAM25899.1; -; Genomic_DNA.
DR RefSeq; WP_009610971.1; NC_003869.1.
DR AlphaFoldDB; Q8R6K9; -.
DR SMR; Q8R6K9; -.
DR STRING; 273068.TTE2795; -.
DR EnsemblBacteria; AAM25899; AAM25899; TTE2795.
DR KEGG; tte:TTE2795; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_9; -.
DR OMA; RYQTATP; -.
DR OrthoDB; 146811at2; -.
DR Proteomes; UP000000555; 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..633
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG 2"
FT /id="PRO_0000117201"
FT BINDING 14..19
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"
SQ SEQUENCE 633 AA; 71062 MW; 0E051590AE5B4916 CRC64;
MRYIAGEYDV CVVGLGHAGS EAALASARLG LATVGFATNL DAIALMACNP SIGGPAKAQL
VREIDALGGE MAVNTDKSLL QMRTLNTSKG PAVRSLRAQV DKKLYQANMK HTLERQKNLD
IKQAEIVDIL VENNKVVGVV TKLGAIYKCK ACIITTGTFL RGRVIIGEVG FESGPSGLFP
AKELSEAIKR LGFKMMRFNT STPPRVDKRT VDFSKMIMQP GDEVITPFSF MHDKIEIEQI
PCWLTYTNEK THKIIRDNIH RAPLYTGEVE GVGVRYCPSI EDKVMKFPHR DRHQIFVEPE
GRDTYEMYIQ GLFSSFPEDL QMEILSTIPG LENAKIMRPA YAIEYDCIDP TQLKATLETK
LVEGLYFAGQ VNGTSGYEEA AAQGLMAGIN AALKILGKPP LILDRSQAYI GILIDDLVTK
GTNEPYRMLT SRAEYRLILR QDNADFRLTE IGKEIGLVTE ERYEKFLRKK IQLEKEMMRL
PTVMVRPTEE VNNFLISRGS TPLVSGVDLY TLLKRPEIDY KSTKFLDPTR PDDILDSVAE
QIDINIKYEG YILKQLRQVE QFKAMENKKI PEDIDYYQVH GLSNEAKEKL SKIRPTSVGQ
ASRISGVSPA DISVLLIYLQ QMRRKRSDEA KIN
