MNMG_HELPY
ID MNMG_HELPY Reviewed; 621 AA.
AC P56138; O32632;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=HP_0213;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 49503 / 60190;
RA Karita M., Etterbeek M.L., Forsyth M.H., Tummuru M.K.R., Blaser M.J.;
RL Submitted (JUL-1997) 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; AE000511; AAD07281.1; -; Genomic_DNA.
DR EMBL; AF008565; AAB63296.1; -; Genomic_DNA.
DR PIR; E64546; E64546.
DR RefSeq; NP_207011.1; NC_000915.1.
DR RefSeq; WP_000238111.1; NC_018939.1.
DR AlphaFoldDB; P56138; -.
DR SMR; P56138; -.
DR DIP; DIP-3538N; -.
DR IntAct; P56138; 1.
DR MINT; P56138; -.
DR STRING; 85962.C694_01070; -.
DR PaxDb; P56138; -.
DR EnsemblBacteria; AAD07281; AAD07281; HP_0213.
DR KEGG; hpy:HP_0213; -.
DR PATRIC; fig|85962.47.peg.230; -.
DR eggNOG; COG0445; Bacteria.
DR OMA; FRPGYAI; -.
DR PhylomeDB; P56138; -.
DR Proteomes; UP000000429; 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..621
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000117112"
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"
FT VARIANT 10
FT /note="V -> I (in strain: 60190)"
FT VARIANT 105
FT /note="L -> F (in strain: 60190)"
FT VARIANT 193
FT /note="D -> E (in strain: 60190)"
FT VARIANT 220
FT /note="T -> A (in strain: 60190)"
FT VARIANT 302
FT /note="S -> N (in strain: 60190)"
FT VARIANT 353
FT /note="T -> A (in strain: 60190)"
FT VARIANT 379
FT /note="A -> D (in strain: 60190)"
FT VARIANT 415
FT /note="I -> V (in strain: 60190)"
FT VARIANT 457
FT /note="E -> Q (in strain: 60190)"
FT VARIANT 480..481
FT /note="YI -> CV (in strain: 60190)"
FT VARIANT 487..488
FT /note="EV -> KL (in strain: 60190)"
FT VARIANT 493
FT /note="D -> N (in strain: 60190)"
FT VARIANT 505
FT /note="D -> N (in strain: 60190)"
SQ SEQUENCE 621 AA; 69684 MW; C5C5CE80259E49E8 CRC64;
MVKESDILVV GGGHAGIEAS LIAAKMGARV HLITMLIDTI GLASCNPAIG GLGKGHLTKE
VDVLGGAMGI ITDHSGLQYR VLNASKGPAV RGTRAQIDMD TYRILARNLV LNTPNLSVSQ
EMTESLILEN DEVVGVTTNI NNTYRAKKVI ITTGTFLKGV VHIGEHQNQN GRFGENASNS
LALNLRELGF KVDRLKTGTC PRVAGNSIDF EGLEEHFGDT NPPYFSYKTK DFNPTQLSCF
ITYTNPITHQ IIRDNFHRAP LFSGQIEGIG PRYCPSIEDK INRFSEKERH QLFLEPQTIH
KSEYYINGLS TSLPLDVQEK VIHSIKGLEN ALITRYGYAI EYDFIQPTEL THTLETKKIK
GLYLAGQING TTGYEEAAAQ GLMAGINAVL ALKNQAPFIL KRNEAYIGVL IDDLITKGTN
EPYRMFTSRA EYRLLLREDN TLFRLGEHAY RLGLMEEDFY KELKKDKQEI QDNLKRLKEY
ILTPSKEVLK RLDELDENPI NDKVDGVSLL ARDSFNAEKM RSFFSFLAPL NERVLEQIKI
ECKYNIYIEK QHENIAKMDS MLKVSIPKGF VFKGIPGLSL EAVEKLEKFR PKSLFEASEI
SGITPANLDV LHLYIHLRKN S
