ID F6IUJ2_LACPE Unreviewed; 637 AA.
AC F6IUJ2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
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 ORFNames=LPE_01263 {ECO:0000313|EMBL:CCB82250.1};
OS Lactiplantibacillus pentosus MP-10.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1028490 {ECO:0000313|EMBL:CCB82250.1};
RN [1] {ECO:0000313|EMBL:CCB82250.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MP-10 {ECO:0000313|EMBL:CCB82250.1};
RX PubMed=21705590; DOI=10.1128/JB.05171-11;
RA Abriouel H., Benomar N., Perez Pulido R., Canamero M.M., Galvez A.;
RT "Annotated genome sequence of Lactobacillus pentosus MP-10, which has
RT probiotic potential, from naturally fermented Alorena green table olives.";
RL J. Bacteriol. 193:4559-4560(2011).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00129}.
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DR EMBL; FR871786; CCB82250.1; -; Genomic_DNA.
DR RefSeq; WP_065674932.1; NZ_FLYG01000003.1.
DR AlphaFoldDB; F6IUJ2; -.
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 554..625
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT BINDING 18..23
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 281..295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 637 AA; 71068 MW; 956A73F524CFE406 CRC64;
MTEVKQYQGR DYDVIVVGAG HAGSEAALAA ARMGNRTLLM TINLDMVAFM PCNPSVGGPA
KGIVVREIDA LGGEMGRNID KTYVQMRMLN TGKGPAVRAL RAQADKHAYH SEMKHTIERE
PNLTLRQGIV DGLIVEDGVC KGVITNTGAH YRAKSVVLTT GTAARGKIII GELMYSSGPN
NSQPAMKLSG DLERLGFKLE RFKTGTPPRV DGNTIDYSVT EEQPGDPEPH HFSFETKDED
YLDLKHQLSC WLTYTNETTH KIIRENLDRA PMFTGVIEGV GPRYCPSIED KIVRFADKKR
HQLFLEPEGR NTDEWYVQGL STSMPEEVQQ RILHSIKGLE DAEMMRPGYA IEYDVVAPYQ
LKATLETKLI KNLYTAGQTN GTSGYEEAAG QGLMAGINAG LRALDRGQFT LKRSDAYIGV
MIDDLVTKGT NEPYRLLTSR AEYRLILRHD NADLRLTDKG RELGLIDDDR YAAFEAKRQA
IKDELDRLGK IRIKPNDDVN AFLRAHNSGE LKDGVLAADF LKRPEVRYAD LMKFIPAAPE
PLERHIIEQV EIQIKYAGYI EKAEERVERL KKMEAKKVPD RIDYDAIDGL ATEAHQKLKK
IQPTTIAQAS RISGVNPADI AILSVYIQQG RIAKVKD
//
