ID V9WD73_9BACL Unreviewed; 631 AA.
AC V9WD73;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG {ECO:0000256|ARBA:ARBA00020461, ECO:0000256|HAMAP-Rule:MF_00129};
DE AltName: Full=Glucose-inhibited division protein A {ECO:0000256|ARBA:ARBA00031800, ECO:0000256|HAMAP-Rule:MF_00129};
GN Name=mnmG {ECO:0000256|HAMAP-Rule:MF_00129,
GN ECO:0000313|EMBL:AHD07779.1};
GN Synonyms=gidA {ECO:0000256|HAMAP-Rule:MF_00129};
GN ORFNames=ERIC2_c41240 {ECO:0000313|EMBL:AHD07779.1};
OS Paenibacillus larvae subsp. larvae DSM 25430.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=697284 {ECO:0000313|EMBL:AHD07779.1, ECO:0000313|Proteomes:UP000029431};
RN [1] {ECO:0000313|EMBL:AHD07779.1, ECO:0000313|Proteomes:UP000029431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25430 {ECO:0000313|EMBL:AHD07779.1,
RC ECO:0000313|Proteomes:UP000029431};
RX PubMed=24599066;
RA Djukic M., Brzuszkiewicz E., Funfhaus A., Voss J., Gollnow K., Poppinga L.,
RA Liesegang H., Garcia-Gonzalez E., Genersch E., Daniel R.;
RT "How to Kill the Honey Bee Larva: Genomic Potential and Virulence
RT Mechanisms of Paenibacillus larvae.";
RL PLoS ONE 9:E90914-E90914(2014).
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, ECO:0000256|HAMAP-Rule:MF_00129}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|HAMAP-Rule:MF_00129};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC {ECO:0000256|ARBA:ARBA00025948, ECO:0000256|HAMAP-Rule:MF_00129}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00129}.
CC -!- SIMILARITY: Belongs to the MnmG family. {ECO:0000256|ARBA:ARBA00007653,
CC ECO:0000256|HAMAP-Rule:MF_00129}.
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DR EMBL; CP003355; AHD07779.1; -; Genomic_DNA.
DR RefSeq; WP_024095532.1; NZ_CP019652.1.
DR AlphaFoldDB; V9WD73; -.
DR KEGG; plv:ERIC2_c41240; -.
DR PATRIC; fig|697284.3.peg.3869; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_9; -.
DR Proteomes; UP000029431; 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 PRINTS; PR00411; PNDRDTASEI.
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 {ECO:0000256|HAMAP-Rule:MF_00129};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_00129};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_00129};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00129};
KW Reference proteome {ECO:0000313|Proteomes:UP000029431};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00129}.
FT DOMAIN 546..617
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT BINDING 14..19
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 126
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 181
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 274..288
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 371
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 631 AA; 70294 MW; CE2D0D97422B24D5 CRC64;
MGFQAGEYDV IVIGAGHAGC ESALAAARMG CSTLLLTINL DMVAFMPCNP SIGGPAKGHV
VREIDALGGE MGRNIDKTYI QIRMLNTGKG PAVHALRAQA DKFLYQQTMK ETIEKQPNLT
MRQGMVEELI VEAGVCKGVI TKSGAEYYGK AIVLTTGTYL RGKVIMGELM YESGPNNQQP
SIKLSESLRN LGFELVRFKT GTPPRVHKES IDFSKTEIQP GDAEPEFFSY ETREPVKEEQ
LPCWLTYTSA ETQELITENL HRAPMFSGVI EGTGPRYCPS IEDKIVRFAD KPKHQIFLEP
EGRYTSEYYV QGLSTSMPED VQLSMLRTIP GLECVEMMRT GYAIEYDAVI PTQLKPTLET
KLVEGLFTAG QINGTSGYEE AAGQGIMAGI NAARKVQGKE PIILDRSEGY IGVLIDDLVT
KGTNEPYRLL TSRAEYRLLL RHDNADLRLT PIGYEIGLIT EERYQAFLNK KGKVEQEIER
LRTTKVRPEA FIQDLLAEAG TVQLNNAVDL LSLLRRPQIM YSHIEQMSPS PLELDGEMKE
QVEIQIKYSG YIEKQLAQVE RLKKMEKKLI PDDIVYEEIH GIATEAKQKL AKIRPISIGQ
ASRISGVSPA DISILLVYLE HYNQVTAARR G
//
