ID D4MX65_ANAHA Unreviewed; 627 AA.
AC D4MX65;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
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:CUN11624.1};
GN Synonyms=gidA {ECO:0000256|HAMAP-Rule:MF_00129};
GN ORFNames=CL2_00940 {ECO:0000313|EMBL:CBL37210.1}, ERS852425_02720
GN {ECO:0000313|EMBL:CUN11624.1}, ERS852520_02334
GN {ECO:0000313|EMBL:CUP84225.1}, ERS852571_02761
GN {ECO:0000313|EMBL:CUN13783.1};
OS Anaerostipes hadrus.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerostipes.
OX NCBI_TaxID=649756 {ECO:0000313|EMBL:CBL37210.1, ECO:0000313|Proteomes:UP000008960};
RN [1] {ECO:0000313|EMBL:CBL37210.1, ECO:0000313|Proteomes:UP000008960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSC/2 {ECO:0000313|EMBL:CBL37210.1,
RC ECO:0000313|Proteomes:UP000008960};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Clostridiales sp. SSC/2.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL37210.1, ECO:0000313|Proteomes:UP000008960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSC/2 {ECO:0000313|EMBL:CBL37210.1,
RC ECO:0000313|Proteomes:UP000008960};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000095553, ECO:0000313|Proteomes:UP000095564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5608868 {ECO:0000313|EMBL:CUN11624.1,
RC ECO:0000313|Proteomes:UP000095598}, 2789STDY5834908
RC {ECO:0000313|EMBL:CUP84225.1, ECO:0000313|Proteomes:UP000095564}, and
RC 2789STDY5834959 {ECO:0000313|EMBL:CUN13783.1,
RC ECO:0000313|Proteomes:UP000095553};
RG Pathogen Informatics;
RL Submitted (SEP-2015) 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}.
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; FP929061; CBL37210.1; -; Genomic_DNA.
DR EMBL; CYXT01000024; CUN11624.1; -; Genomic_DNA.
DR EMBL; CYXY01000021; CUN13783.1; -; Genomic_DNA.
DR EMBL; CZAU01000024; CUP84225.1; -; Genomic_DNA.
DR RefSeq; WP_008392988.1; NZ_WQRA01000001.1.
DR AlphaFoldDB; D4MX65; -.
DR STRING; 649756.ERS852387_02322; -.
DR GeneID; 15230301; -.
DR KEGG; bprl:CL2_00940; -.
DR PATRIC; fig|245018.3.peg.1186; -.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000008960; Chromosome.
DR Proteomes; UP000095553; Unassembled WGS sequence.
DR Proteomes; UP000095564; Unassembled WGS sequence.
DR Proteomes; UP000095598; 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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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 547..618
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT COILED 465..499
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 14..19
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 275..289
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 627 AA; 70318 MW; 9C94EC1A30074234 CRC64;
MNNLEEKYDI IVVGAGHAGC EAALAAARMG FETICFTVSM DSVALMPCNP NIGGSSKGHL
VKEIDALGGE MGKNIDKTYL QSKMLNKSKG PAVHSLRAQA DKKMYSISMT QVMGNTPNLT
LRQGEVTEIL VEDGKIKGVK TYSGAVYYAK AVVLTTGTYL KARCIYGEVS NHTGPNGLQA
ANYLTDSLKS HGISMRRFKT GTPARIDKNT IDFSKMAEQF GDERIVPFSF TNKEEDIKRD
QISCWLTYTT EETHEIIKEN IHRSPLFSGA IEGTGPRYCP SIEDKIVKFP DKNRHQVFIE
PEGEYTNEMY VGGMSSSLPE DVQYKMYHSV PGLENAKIVR NAYAIEYDCI DATQLKASLE
FKEIDGLFSG GQFNGSSGYE EAAAQGLMAG INAARKLQEK DPIILDRSQA YIGVLIDDLV
TKETQEPYRM MTSRAEYRLL LRQDNADLRL TKIGYEAGLI SQERYDKLLV KEQQIEDEMK
RLEDINVGAS KNVQSLLEEL GSTTLKSSAK MTELIRRPEL TYMDLAPIDP ERPEYDLDVQ
EQVNINIKYE GYIKRQLSQV KQFKKMEKKR IPEDIDYEDV GSLRIEAKQK LSKIRPSSIG
QASRISGVSP ADISVLLIYL EQMHHRR
//
