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Database: UniProt
Entry: M5J6R8_9LACO
LinkDB: M5J6R8_9LACO
Original site: M5J6R8_9LACO 
ID   M5J6R8_9LACO            Unreviewed;       641 AA.
AC   M5J6R8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 50.
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=D271_00858 {ECO:0000313|EMBL:EKW99640.1};
OS   Ligilactobacillus saerimneri 30a.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1227363 {ECO:0000313|EMBL:EKW99640.1, ECO:0000313|Proteomes:UP000011912};
RN   [1] {ECO:0000313|EMBL:EKW99640.1, ECO:0000313|Proteomes:UP000011912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=30a {ECO:0000313|EMBL:EKW99640.1,
RC   ECO:0000313|Proteomes:UP000011912};
RX   PubMed=23405290;
RA   Romano A., Trip H., Campbell-Sills H., Bouchez O., Sherman D.,
RA   Lolkema J.S., Lucas P.M.;
RT   "Genome Sequence of Lactobacillus saerimneri 30a (Formerly Lactobacillus
RT   sp. Strain 30a), a Reference Lactic Acid Bacterium Strain Producing
RT   Biogenic Amines.";
RL   Genome Announc. 1:E00097-E00012(2013).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKW99640.1}.
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DR   EMBL; ANAG01000003; EKW99640.1; -; Genomic_DNA.
DR   RefSeq; WP_009551250.1; NZ_ANAG01000003.1.
DR   AlphaFoldDB; M5J6R8; -.
DR   STRING; 1227363.D271_00858; -.
DR   GeneID; 80986086; -.
DR   PATRIC; fig|1227363.6.peg.165; -.
DR   Proteomes; UP000011912; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000011912};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00129}.
FT   DOMAIN          557..628
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme C-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01228"
FT   BINDING         20..25
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT   BINDING         283..297
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   641 AA;  71034 MW;  01598B390D8E7302 CRC64;
     MVESFGKQYQ GQDYDVIVVG AGHAGCEAAL AAARMGNETL LITIQLEMTA FMPCNPSIGG
     PAKGIVVREV DALGGEMGRN IDKTYVQMRM LNTGKGPAVR ALRAQADKRL YSEEMKHTLE
     RQEHLTLRQG IVDDLIVEDG VVKGVITNTG ARYGAKAVVL TTGTAARGRI IIGELRYSSG
     PNNTQAAVEL SKNLEKLGFE LKRFKTGTPP RVDGNTIDYS KTEEQPGDAD VNHFSFETSD
     EDYLTVEQQL SCWLTYTNEK THEIINSNLD RAPMFSGVIE GVGPRYCPSI EDKIVRFADK
     PRHQLFLEPE GRNTDEYYVQ GLSTSMPEEV QQQMVHSISG LENAQMMRPG YAIEYDIVAP
     YQLRPTLETK LIRGLYTAGQ TNGTSGYEEA AGQGIIAGIN AGRHALGKEE IVLKRSDAYI
     GVMIDDLVTK GTNEPYRLLT SRAEYRLILR HDNADLRLTD LGHEIGLISD ERYQAFEAKK
     AAITAEEARL ATIRLTPNTP GINDYLEAHG DRPLKDGVLA SDFLRRPYAS YKDLLQFIPA
     PAEPLDRRVI EQIEIQFKYA GYIKKEEEKV AKLKRMEAKK IPADIDYAKI DGIATEARQK
     FEKIQPTTLA QAGRISGVNP ADLAILAVYI QEGRIAKKQA E
//
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