ID MNMG_CAMJE Reviewed; 619 AA.
AC Q9PNA7; Q0P968;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 118.
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=Cj1188c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; AL111168; CAL35303.1; -; Genomic_DNA.
DR PIR; F81324; F81324.
DR RefSeq; WP_002864546.1; NZ_SZUC01000001.1.
DR RefSeq; YP_002344579.1; NC_002163.1.
DR AlphaFoldDB; Q9PNA7; -.
DR SMR; Q9PNA7; -.
DR IntAct; Q9PNA7; 12.
DR STRING; 192222.Cj1188c; -.
DR PaxDb; 192222-Cj1188c; -.
DR EnsemblBacteria; CAL35303; CAL35303; Cj1188c.
DR GeneID; 905478; -.
DR KEGG; cje:Cj1188c; -.
DR PATRIC; fig|192222.6.peg.1169; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_7; -.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000000799; 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; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.150.570; GidA associated domain, C-terminal subdomain; 1.
DR Gene3D; 1.10.10.1800; tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG/GidA; 1.
DR HAMAP; MF_00129; MnmG_GidA; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR049312; GIDA_C_N.
DR InterPro; IPR004416; MnmG.
DR InterPro; IPR002218; MnmG-rel.
DR InterPro; IPR020595; MnmG-rel_CS.
DR InterPro; IPR026904; MnmG_C.
DR InterPro; IPR047001; MnmG_C_subdom.
DR InterPro; IPR044920; MnmG_C_subdom_sf.
DR InterPro; IPR040131; MnmG_N.
DR NCBIfam; TIGR00136; gidA; 1.
DR PANTHER; PTHR11806; GLUCOSE INHIBITED DIVISION PROTEIN A; 1.
DR PANTHER; PTHR11806:SF0; PROTEIN MTO1 HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF01134; GIDA; 1.
DR Pfam; PF13932; GIDA_C; 1.
DR Pfam; PF21680; GIDA_C_1st; 1.
DR SMART; SM01228; GIDA_assoc_3; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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..619
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000117077"
FT BINDING 8..13
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 267..281
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 619 AA; 69172 MW; 18261C2019852AE2 CRC64;
MFDVIVIGGG HAGVEASAAA ARMGKKTLLL TTLIEQIGAA SCNPAIGGLA KGHLVKELDA
MGGLMGEITD EAGIQFRILN ESKGVAVQGS RAQIDMDKYR IIARNKLLKL PNLEISQEQA
SVLIVENDEV KGVKTNLENI YFAKKVILTT GTFLNGLIHV GENKLQAGRV GELASVNLGN
YLQTLGLKMG RLKTGTCPRV DAKSIDFSVL EIQDGDVNPK AFSFRSRNFN PTQLPCYIAR
TNTTTHEIIK NNFYRAPLFT GQIEGVGPRY CPSIEDKINR FSDKESHHLF IEPQTIDATE
YYINGFSTSL PYEVQTQMLR SVEGFENAKI TRFGYAIEYD YIEPTELKHT LELKKIKNLY
CAGQINGTTG YEEAAAQGFM AGINASLSID MKEPLILRRD EAYIGVLIDD LVVKGTKEPY
RMFTSRAEFR LLLREENAIL RLGKYGYDLG LLSEQDFTYI QNIANNLQKG LEFLLSKEFT
PNNQNNAFLE SLGEDKISSI VNLQKIVARA SFDIEKLKKL DPIFETMDHY SLREILNEAK
YYHYISMQKA QVEKMKNLSE LKIPENFDFK SVSGLSNEVV EKLNHHKPPT IFAASQISGI
TPAALDILQI YIKMQKKKA
//
