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Database: UniProt
Entry: A0A1I6NVP5_9BACI
LinkDB: A0A1I6NVP5_9BACI
Original site: A0A1I6NVP5_9BACI 
ID   A0A1I6NVP5_9BACI        Unreviewed;       630 AA.
AC   A0A1I6NVP5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=SAMN05421668_10120 {ECO:0000313|EMBL:SFS32042.1};
OS   Halolactibacillus miurensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halolactibacillus.
OX   NCBI_TaxID=306541 {ECO:0000313|EMBL:SFS32042.1, ECO:0000313|Proteomes:UP000199139};
RN   [1] {ECO:0000313|EMBL:SFS32042.1, ECO:0000313|Proteomes:UP000199139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17074 {ECO:0000313|EMBL:SFS32042.1,
RC   ECO:0000313|Proteomes:UP000199139};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FPAI01000001; SFS32042.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6NVP5; -.
DR   STRING; 306541.SAMN05421668_10120; -.
DR   OrthoDB; 9815560at2; -.
DR   Proteomes; UP000199139; 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; 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          544..615
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         180
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT   BINDING         272..286
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT   BINDING         369
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   630 AA;  70350 MW;  0CBB69A4719B6517 CRC64;
     MYNAGHYDVI VVGAGHAGVE AAHAAVKRGA KTLMLSLNLD MIAFMPCNPS IGGPAKGVVV
     REIDALGGLM GKVIDKTYIQ MRMLNTGKGP AVRALRAQAD KPLYIQEMKY QLEQLDNLTM
     RQAMVEELIV EDGEVKGVLT ETKAAYYAKS VIITTGTFMR GRVIIGDVSY ESGPNNQRAS
     IKLAENLESL GFDIVRFKTG TPPRVNSRSI DYSKTEIQPG DDNPRHFSYE TTEMIVDQIP
     CWLTYTTEET HEIINENLGL SAMYSGMIKG TGPRYCPSIE DKVVRFHDKP RHQIFLEPEG
     RDTEEVYVQG FSTSLPEFVQ HKMLRSIPGL EEAEIMRSGY AIEYDAVVPT QLWPTLEVKS
     ISGLYTAGQI NGTSGYEEAA GQGLMAGINA AAHALSLETL ILDRSQAYIG VLIDDLVTKG
     TNEPYRLLTS RAEYRLLLRH DNADLRLTKL GHDLGLISNE RYESFEQKLA AIEDEQKRLS
     KIVIKPNDEL NAILQEIGET DLKEPLKALE LMKRPKVTYD VIERILEEDS SLDIDVKEQV
     EIQVKYEGYI TKSRQQVDRM KKMENKVIPE DIDYSAISGL ATEARQKLEK VRPLSVGQAS
     RISGVNPADV SILLVYIEQG QIKRLSEDER
//
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