MNMG_CHLTR
ID MNMG_CHLTR Reviewed; 610 AA.
AC P0CD73; O84506;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 55.
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}; OrderedLocusNames=CT_498;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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; AE001273; AAC68099.1; -; Genomic_DNA.
DR PIR; H71503; H71503.
DR RefSeq; NP_220013.1; NC_000117.1.
DR RefSeq; WP_010725215.1; NC_000117.1.
DR AlphaFoldDB; P0CD73; -.
DR SMR; P0CD73; -.
DR STRING; 813.O172_02750; -.
DR EnsemblBacteria; AAC68099; AAC68099; CT_498.
DR GeneID; 884271; -.
DR KEGG; ctr:CT_498; -.
DR PATRIC; fig|272561.5.peg.542; -.
DR HOGENOM; CLU_007831_2_2_0; -.
DR InParanoid; P0CD73; -.
DR OMA; FRPGYAI; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
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..610
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000117083"
FT BINDING 14..19
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 274..288
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 610 AA; 67202 MW; 6FF516182E49B49D CRC64;
MWTFPVDYDV IVIGAGHAGC EAAYCAAKMG ASVLLLTSNL DTIAKLSCNP AVGGIGKGHI
VREIDALGGI MAEITDLSGI QFRILNQTKG PAVRAPRAQV DKQLYHIHMK RLLEQVPGLH
IMQGTAEALL DNGEKVLGVS TKEGWAYLGK TVVLSSGTFM RGLIHIGTQN FSGGRLGDAA
SLGLSEDLKR LGFPLGRLKT GTPARLLASS IDFSVMEEQP GDHNVCFVHR NEMFVPTLPQ
VSCHITHTTD QTKDLITKNL HRSALYGGRI EGVGPRYCPS IEDKIVKFAD KDRHHIFIEP
EGLNTQEVYV NGLSTSMPFD VQYDIIRSVS GLENAIITRP AYAIEYDYVH GNVIFPSLES
KLIEGLFLCG QINGTTGYEE AAAQGLIAGV NAVNKVLRHP PFVPSRQESY IGVMLDDLTT
QVLDEPYRMF TSRAEHRLLL RQDNAGMRLS HYGHSLGLLS SERYAMFQEQ KACIEQEKER
LSKTFRKYGD TVVPLTKVLC RPEVSYQQLL TEFPADVRDL GPVVGASLEM EIKYSGYISR
QQTLIRSMER SENISIPEDI DYHSISALSL EAREKLSKFT PRTIGSAARI SGISVADIQV
LMVSLKKDAH