MNMG_HELAH
ID MNMG_HELAH Reviewed; 621 AA.
AC Q17VU9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=Hac_1506;
OS Helicobacter acinonychis (strain Sheeba).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=382638;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sheeba;
RX PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA Gressmann H., Achtman M., Schuster S.C.;
RT "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT host jump from early humans to large felines.";
RL PLoS Genet. 2:1097-1110(2006).
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; AM260522; CAK00227.1; -; Genomic_DNA.
DR RefSeq; WP_011578314.1; NC_008229.1.
DR AlphaFoldDB; Q17VU9; -.
DR SMR; Q17VU9; -.
DR STRING; 382638.Hac_1506; -.
DR EnsemblBacteria; CAK00227; CAK00227; Hac_1506.
DR KEGG; hac:Hac_1506; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_7; -.
DR OMA; FRPGYAI; -.
DR OrthoDB; 146811at2; -.
DR BioCyc; HACI382638:HAC_RS06385-MON; -.
DR Proteomes; UP000000775; 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..621
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_1000016609"
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; 69651 MW; 9F734CAB11E80F7A CRC64;
MVKESDILVV GGGHAGIEAS LIAAKMGAKT HLITMLIDTI GLASCNPAIG GLGKGHLTKE
VDVLGGAMGI ITDNSGLQYR VLNASKGPAV RGTRAQIDMD TYRIFARNLV LNTPNLSVSQ
EMTESLIIEN DEVVGVTTNI NNTYRAKKVI ITTGTFLKGV VHIGEHQNQN GRFGENASNS
LALNLRELGF KVERLKTGTC PRVAGKSINF EGLEEHFGDT NPPYFSYKTK NFNPTQLSCF
ITYTNPTTHQ IIRDNFHRAP LFSGQIEGIG PRYCPSIEDK INRFSEKERH QLFLEPQTIH
KSEYYINGLS TSLPLDVQEE TIHSIKGLEN ALITRYGYAI EYDFIQPTEL THTLETKKIK
GLYLAGQING TTGYEEAAAQ GLMAGINAVL ALKNQAPFIL KRNEAYIGVL IDDLVTKGTN
EPYRMFTSRA EYRLLLREDN TLFRLGEHAY HLGLMEKDFY KELKKDKQEI QENLKRLKEC
VLTPSKEVLK RLSELDENPI NDKINGVDLL ARDSFSLEKM RSFFSFLAPL SERVLEQIKI
ECKYNIYIEK QHENIAKMDS MLKVSIPKDF VFKGIPGLSL EAVEKLEKFR PKSLFEASEI
SGITPANLDV LHLYIHLRKN S