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MNMG1_CALS4
ID   MNMG1_CALS4             Reviewed;         633 AA.
AC   Q8RAT8;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG 1 {ECO:0000255|HAMAP-Rule:MF_00129};
DE   AltName: Full=Glucose-inhibited division protein A 1 {ECO:0000255|HAMAP-Rule:MF_00129};
GN   Name=mnmG1 {ECO:0000255|HAMAP-Rule:MF_00129};
GN   Synonyms=gidA1 {ECO:0000255|HAMAP-Rule:MF_00129};
GN   OrderedLocusNames=TTE1110;
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; AAM24348.1; -; Genomic_DNA.
DR   RefSeq; WP_011025458.1; NC_003869.1.
DR   AlphaFoldDB; Q8RAT8; -.
DR   SMR; Q8RAT8; -.
DR   STRING; 273068.TTE1110; -.
DR   EnsemblBacteria; AAM24348; AAM24348; TTE1110.
DR   KEGG; tte:TTE1110; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_9; -.
DR   OMA; FRPGYAI; -.
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 1"
FT                   /id="PRO_0000117200"
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;  71072 MW;  57895890E08C4477 CRC64;
     MRFVAGEYDV CVVGLGHAGS EAALASARLG LSTVGFATNL DAIALMACNP SIGGPAKAQL
     VREIDALGGQ MAINTDKSLL QMRTLNTSKG PAVRSLRAQV DKKLYQMNMK HTLERQENLD
     IKQAEIVDIL VEDNKVTGVV TKLGAIYKCK ACIITTGTFL KGRVIIGEVD FESGPSGLFP
     ASELSEALKR LGFKLMRFKT GTPPRVDKRS IDFSKMEIQP GDEVITPFSF MHDKIEIEQM
     PCWLTYTNEK THKIIRDNIH RAPLFTGAIT GVGVRYCPSI EDKVVKFPHR ERHQIFIEPE
     GRDTYEMYVQ GMSSSLPEDV QLEFLRTVPG LENVRVMRPA YAIEYDCIDP TQLKATLESK
     WIEGLYFAGQ VNGTSGYEEA AAQGLMAGIN AAMKILNKPP VVLDRSQAYI GILIDDLVTK
     GTNEPYRMLT SRAEYRLLLR QDNADFRLTE IGKEIGLVTE ERYEKFLRKK IQLEKEMRRL
     STVMVRPTEE VNNFLISRGS TPLVSGVDLY TLLKRPEVDY KSTKFLDPDR PDDILDSVAE
     QIDINIKYEG YILKQLRQVE QFKAMENKKI PEDIDYYQIS GLSNEAKEKL SKIRPTSVGQ
     ASRISGVSPA DISVLLIYLQ QMRKKKSNES RIS
 
 
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