ID Q6J5H6_HAEIF Unreviewed; 330 AA.
AC Q6J5H6;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 63.
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:AAT40770.1};
OS Haemophilus influenzae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=727 {ECO:0000313|EMBL:AAT40770.1};
RN [1] {ECO:0000313|EMBL:AAT40770.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15908377; DOI=10.1128/IAI.73.6.3479-3491.2005;
RA Shen K., Antalis P., Gladitz J., Sayeed S., Ahmed A., Yu S., Hayes J.,
RA Johnson S., Dice B., Dopico R., Keefe R., Janto B., Chong W., Goodwin J.,
RA Wadowsky R.M., Erdos G., Post J.C., Ehrlich G.D., Hu F.Z.;
RT "Identification, distribution, and expression of novel genes in 10 clinical
RT isolates of nontypeable Haemophilus influenzae.";
RL Infect. Immun. 73:3479-3491(2005).
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; AY599430; AAT40770.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6J5H6; -.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR Gene3D; 2.40.30.260; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; 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 SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
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 8..330
FT /note="MnmG N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01134"
FT NON_TER 330
FT /evidence="ECO:0000313|EMBL:AAT40770.1"
SQ SEQUENCE 330 AA; 36073 MW; C188B5FEF94E3836 CRC64;
MFYTETYDVI VIGGGHAGTE AALAPARMGF KTLLLTHNVD TLGQMSCNPA IGGIGKGHLV
KEVDAMGGLM AHAADKAGIQ FRTLNSSKGP AVRATRAQAD RVLYRQAVRT ALENQPNLDI
FQQEATDILI EQDRVTGVST KMGLIFRAKS VVLTAGTFLA GKIHIGLENY EGGRAGDPAS
VNLSHRLRDL GLRVDRLKTG TPPRIDARTI NFDILAKQHG DEVLPMFSFM GSVDDHPQQI
PCYITYTNEQ THEVIRNNLD RSPMYTGVIE GIGPRYCPSI EDKVMRFSDR NSHQIYLEPE
GLTSNEVYPN GISTSLPFDV QMGIVNSMKG
//
