MNMG_HELPS
ID MNMG_HELPS Reviewed; 621 AA.
AC B2US42;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=HPSH_01100;
OS Helicobacter pylori (strain Shi470).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=512562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shi470;
RA Kersulyte D., Kalia A., Gilman R.H., Berg D.E.;
RT "Genome sequence of Helicobacter pylori from the remote Amazon: traces of
RT Asian ancestry of the first Americans.";
RL Submitted (MAY-2008) 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}.
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DR EMBL; CP001072; ACD47674.1; -; Genomic_DNA.
DR RefSeq; WP_000238021.1; NC_010698.2.
DR AlphaFoldDB; B2US42; -.
DR SMR; B2US42; -.
DR KEGG; hps:HPSH_01100; -.
DR HOGENOM; CLU_007831_2_2_7; -.
DR OMA; FRPGYAI; -.
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..621
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_1000095654"
FT BINDING 11..16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 270..284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 621 AA; 69710 MW; 537EEB6FFD586DA2 CRC64;
MVKESDILVI GGGHAGIEAS LIAAKMGARV HLITMLIDTI GLASCNPAIG GLGKGHLTKE
VDVLGGAMGI ITDNSGLQYR VLNASKGPAV RGTRAQIDMD TYRIFARNLV LNTPNLSVSQ
EMTESLIIEN DEMVGVTTNI NNTYKAKKVI ITTGTFLKGV VHIGEHQNQN GRFGENASNS
LALNLRELGF RVERLKTGTC PRVAGNSIDF EGLEEHFGDT NPPYFSYKTK DFNPTQLSCF
ITYTNPITHQ IIRDNFHRAP LFSGQIEGIG PRYCPSIEDK INRFSEKERH QLFLEPQTIH
KSEYYINGLS TSLPLDVQEK VIHSIKGLEN ALITRYGYAI EYDFIQPTEL THTLETKKIK
GLYLAGQING TTGYEEAAAQ GLMAGINAVL ALKNQDPFIL KRNEAYIGVL IDDLVTKGTN
EPYRMFTSRA EYRLLLREDN TLFRLGEHAY RLGLMEEDFY KGLKKDQQEI QDNLKRLKEC
VLTPSKEVLK RLNELDENPI NDKVDGVSLL ARDSFNLEKM RSFFSFLTPL NERVLEQIKI
ECKYNIYIEK QHENIAKMDS MLKVSIPKGF VFKGIPGLSL EAVEKLEKFR PKSLFEASEI
SGITPANLDV LHLYIHLRKN S