ID   Q6VP37_9ENTR            Unreviewed;       590 AA.
AC   Q6VP37;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG {ECO:0000256|ARBA:ARBA00020461};
DE   AltName: Full=Glucose-inhibited division protein A {ECO:0000256|ARBA:ARBA00031800};
DE   Flags: Fragment;
GN   Name=gidA {ECO:0000313|EMBL:AAR99281.1};
OS   Candidatus Blochmannia nearcticus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Blochmannia.
OX   NCBI_TaxID=251545 {ECO:0000313|EMBL:AAR99281.1};
RN   [1] {ECO:0000313|EMBL:AAR99281.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Cnear35 {ECO:0000313|EMBL:AAR99281.1};
RX   PubMed=14965905; DOI=10.1080/10635150490264842;
RA   Degnan P.H., Lazarus A.B., Brock C.D., Wernegreen J.J.;
RT   "Host-symbiont stability and fast evolutionary rates in an ant-bacterium
RT   association: cospeciation of camponotus species and their endosymbionts,
RT   candidatus blochmannia.";
RL   Syst. Biol. 53:95-110(2004).
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.
CC       {ECO:0000256|ARBA:ARBA00003717}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC       {ECO:0000256|ARBA:ARBA00025948}.
CC   -!- SIMILARITY: Belongs to the MnmG family.
CC       {ECO:0000256|ARBA:ARBA00007653}.
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DR   EMBL; AY334430; AAR99281.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6VP37; -.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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; 2.
DR   PROSITE; PS01280; GIDA_1; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          506..577
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme C-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01228"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAR99281.1"
SQ   SEQUENCE   590 AA;  66203 MW;  71B1E5164645F2B2 CRC64;
     GQMSCNPAIG GIGKGHLVKE IDAMGGLMAC AIDESGIQFR KLNSSKGVAV RATRAQADKI
     LYRQVIRNKL EYQECLLIVQ ASVEDLIIEN NKIVGVITPK IGMKFRAMSV VLTTGTFLNG
     RIYIGLNNFS GGRAGDIGSS SLLSIRLKEL SSRVGRLKTG TSPRIHSKGV NFDCLHKQHS
     DNPVPVFSFI GSVEQHPRQV PCYITHTNSK THDIVRSNLH QSPMYSGLMK GVSPRYCPSI
     EDKVVRFSDR SAHQIFLEPE GLTTPEIYLN GISTSLPFNI QIQMIKSVQG LENANIIRPG
     YAIEYDFFDP RDLKLTLESK FISGLFFSGQ INGTTGYEEA AAQGLLAGIN AARFSQDKEG
     WYPRRDQAYL GVLVDDLCTH GTEEPYRMFT SRAEYRLSLR EDNADLRLTA IAYRFGLIDE
     FLWENFCRKK EKIEKELQRL RNTYIAPHSV DAKQLNALLK TPLTHEINGA ELLKRPEISY
     IKLSQLSVFG LSELDKQVFD QIEIQIKYEG YIRRQQEDID RYLCNENTLL PINMDFNIVS
     GLSREVIEKL NQCRPCSIGQ ASRIPGITPA AISNLLVWLK KQGLLKSGIF
//