MNMG_CHLTA
ID MNMG_CHLTA Reviewed; 610 AA.
AC Q3KLJ9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=CTA_0546;
OS Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=315277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-571B / DSM 19440 / HAR-13;
RX PubMed=16177312; DOI=10.1128/iai.73.10.6407-6418.2005;
RA Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT genitotropic strains.";
RL Infect. Immun. 73:6407-6418(2005).
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; CP000051; AAX50773.1; -; Genomic_DNA.
DR RefSeq; WP_011324754.1; NC_007429.1.
DR AlphaFoldDB; Q3KLJ9; -.
DR SMR; Q3KLJ9; -.
DR EnsemblBacteria; AAX50773; AAX50773; CTA_0546.
DR KEGG; cta:CTA_0546; -.
DR HOGENOM; CLU_007831_2_2_0; -.
DR OMA; FRPGYAI; -.
DR Proteomes; UP000002532; 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; tRNA processing.
FT CHAIN 1..610
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_1000016579"
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; 67188 MW; C7C72C101C76B49B CRC64;
MWTFPVDYDV IVIGAGHAGC EAAYCAAKMG ASVLLLTSNL DTVAKLSCNP 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