MNMG_ALKHC
ID MNMG_ALKHC Reviewed; 632 AA.
AC Q9RCA8; Q9K5M7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 119.
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=BH4061;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=10427704; DOI=10.1271/bbb.63.1134;
RA Takami H., Masui N., Nakasone K., Horikoshi K.;
RT "Replication origin region of the chromosome of alkaliphilic Bacillus
RT halodurans C-125.";
RL Biosci. Biotechnol. Biochem. 63:1134-1137(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB013492; BAA82679.1; -; Genomic_DNA.
DR EMBL; BA000004; BAB07780.1; -; Genomic_DNA.
DR PIR; E84157; E84157.
DR RefSeq; WP_010900185.1; NC_002570.2.
DR AlphaFoldDB; Q9RCA8; -.
DR SMR; Q9RCA8; -.
DR STRING; 272558.10176686; -.
DR EnsemblBacteria; BAB07780; BAB07780; BAB07780.
DR KEGG; bha:BH4061; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_9; -.
DR OMA; FRPGYAI; -.
DR OrthoDB; 146811at2; -.
DR Proteomes; UP000001258; 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; Reference proteome; tRNA processing.
FT CHAIN 1..632
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000117052"
FT BINDING 14..19
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 126
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 181
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"
FT BINDING 370
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT CONFLICT 572..632
FT /note="EDLDYDAINGLATEAKQKLSEVRPLSVGQASRVSGVNPSDISILLVYLEQGR
FT LAKLGKKTV -> RRLGLRCD (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 632 AA; 69962 MW; 43804419329C96B6 CRC64;
MSYQGGEFDV IVVGAGHAGV EAGLAAARMG ANTLMLTLNL DAVAFMPCNP SVGGPAKGIV
VREIDALGGE MARNIDKTHI QMRMLNTGKG PAVRALRAQA DKFLYQHEMK KTIEEEENLL
LRQGMVERLI IEDGECRGVI TNTGAEYRAK AVVVTTGTYL RGKIIIGDLA YESGPNNMQP
SINLSYHLQE LGFEMVRFKT GTPPRVNGET IDYDKTEIQP GDEVPRAFSY ETTKYITDQL
PCWLTYTGDK THQIINDNLG RSPMYSGMIE GTGPRYCPSI EDKIVRFNDK PRHQIFLEPE
GRHTSEVYVQ GLSTSLPEDV QLDVLKSIPG LEKARMMRPG YAIEYDAIVP TQLWPTLETK
KVPGLFTAGQ INGTSGYEEA AGQGIMAGIN AALRVQGKDG LILDRSEAYI GVLIDDLVTK
GTNEPYRLLT SRAEYRLLLR HDNADLRLTE KGYEIGLIAR ERYERFCEKK AQIAAEKKRL
ESITVKPSKE VNALLEEVGS APLKEAVQAN VFLKRPEVTY EHVAKVIPAP EQELSADVAE
QVEIQIKYEG YISKMLQQVE RAKKMNDKKI PEDLDYDAIN GLATEAKQKL SEVRPLSVGQ
ASRVSGVNPS DISILLVYLE QGRLAKLGKK TV
