ID D2BLG5_LACLK Unreviewed; 625 AA.
AC D2BLG5;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 85.
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 Synonyms=gidA {ECO:0000256|HAMAP-Rule:MF_00129,
GN ECO:0000313|EMBL:ADA65615.1};
GN OrderedLocusNames=LLKF_2040 {ECO:0000313|EMBL:ADA65615.1};
OS Lactococcus lactis subsp. lactis (strain KF147).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=684738 {ECO:0000313|EMBL:ADA65615.1, ECO:0000313|Proteomes:UP000001886};
RN [1] {ECO:0000313|EMBL:ADA65615.1, ECO:0000313|Proteomes:UP000001886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KF147 {ECO:0000313|EMBL:ADA65615.1,
RC ECO:0000313|Proteomes:UP000001886};
RX PubMed=18039825; DOI=10.1128/AEM.01850-07;
RA Siezen R.J., Starrenburg M.J., Boekhorst J., Renckens B., Molenaar D.,
RA van Hylckama Vlieg J.E.;
RT "Genome-scale genotype-phenotype matching of two Lactococcus lactis
RT isolates from plants identifies mechanisms of adaptation to the plant
RT niche.";
RL Appl. Environ. Microbiol. 74:424-436(2008).
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; CP001834; ADA65615.1; -; Genomic_DNA.
DR RefSeq; WP_012898415.1; NC_013656.1.
DR AlphaFoldDB; D2BLG5; -.
DR KEGG; llk:LLKF_2040; -.
DR HOGENOM; CLU_007831_2_2_9; -.
DR Proteomes; UP000001886; 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; PR00368; FADPNR.
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 tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00129}.
FT DOMAIN 549..620
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT BINDING 13..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 276..290
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 373
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 625 AA; 69461 MW; 065EDEFE45423459 CRC64;
MNFQENYDVV VIGGGHAGVE ASLAAARMGS KTLLMTINLN MVAFMPCNPS IGGSAKGIVV
REIDALGGEM GRNIDKTYIQ MKMLNTGKGP AVRALRAQAD KDEYATSMKN TVSDQENLTL
RQGMVEELIL DEEKKKVIGI KTSTGTKYGA KTVIITTGTA LRGEIIIGEL KYSSGPNNSL
SSIGLADNLR EIGFEIGRFK TGTPPRVLAS SIDYDKTEIQ PGDEAPNHFS FMSSDENYLK
DQIPCWLTYT TENSHTILRD NLHRAPLFSG IVKGVGPRYC PSIEDKITRF ADKPRHQLFL
EPEGRNTEEV YIGGLSTSMP EDVQFDLVKS IPGLENAQMM RPGYAIEYDV VMPHQLRPTL
ETKLVSGLFT AGQTNGTSGY EEAAGQGLVA GINAALKVQG KPEFILKRSE AYIGVMIDDL
VTKGTLEPYR LLTSRAEYRL ILRHDNADRR LTEIGRQVGL VSDEQWEHYQ AKMAQFDREM
KRLNSEKLKP LPDTQEKLGK LGFGPIKDAL TGAEFLKRPE VHYNEVIDFI GQAPEKIDRT
VIELIETEIT YEGYIKKAMD QVDKMHRLEA KRIPKNMDWD KLDSIATEAR QKFKKINPET
LGQASRISGV NPADISILMV YLEGK
//
