ID MNMG_ACIBT Reviewed; 626 AA.
AC A3M6R5;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 24-JAN-2024, entry version 88.
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=A1S_2182;
OS Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS KC755 / 5377).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=400667;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX PubMed=17344419; DOI=10.1101/gad.1510307;
RA Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA Gerstein M., Snyder M.;
RT "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT density pyrosequencing and transposon mutagenesis.";
RL Genes Dev. 21:601-614(2007).
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; CP000521; ABO12609.2; -; Genomic_DNA.
DR RefSeq; WP_000559185.1; NZ_CP053098.1.
DR AlphaFoldDB; A3M6R5; -.
DR SMR; A3M6R5; -.
DR KEGG; acb:A1S_2182; -.
DR HOGENOM; CLU_007831_2_2_6; -.
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; tRNA processing.
FT CHAIN 1..626
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000345235"
FT BINDING 13..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 273..287
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 626 AA; 69102 MW; B0FD58FD9D748172 CRC64;
MHYPKVYDVI VIGGGHAGTE AALAAARMGR QTLLLTHNIE TLGQMSCNPA IGGIGKSHLV
REIDALGGAM ALAADKGGIQ FRILNSRKGA AVRATRAQAD RVRYKAAIRE TLENQANLDI
FQQAADDLIV EGDTVKGVVT QMGIRFDAKT VVLTTGTFLG GVIHVGLEKS SGGRAGDPPS
IALAQRLREL KLPVGRLKTG TPPRIDARSV DFSVMTPQPG DFPSPVMSFM GDVSMHPEQV
NCYITHTNEK THDIIRGGLD RSPMYTGVIE GVGPRYCPSI EDKIHRFSDK DSHQVFLEPE
GLDTHELYPN GISTSLPFDV QFELVRSIRG MENAHILRPG YAIEYDYFNP QALKFTLETK
AINGLYFAGQ INGTTGYEEA GAQGLLAGLN AARRAWEQEE WTPKRDQAYM GVLVDDLITL
GTKEPYRMFT SRAEYRLMLR EDNADQRLTT IGRELGLVDD VRWAAYCEKM EAVERETSRL
QHLWAAPNNP MGKKFVEMTG ADLSKECSAI DLLKRPNINF SQIAELTGSE VSQQVGEQIE
IAVKYEGYIN RQHEDVAQLK RLEETKIPAD FDYDVVSGLS REITQKLKTV RPETLAQASR
IPGVTPAAVQ LVMITIRKNN MTKKTA
//
