ID D4JWQ6_9FIRM Unreviewed; 625 AA.
AC D4JWQ6;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 69.
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=EUS_25800 {ECO:0000313|EMBL:CBK97525.1};
OS [Eubacterium] siraeum 70/3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Oscillospiraceae incertae sedis.
OX NCBI_TaxID=657319 {ECO:0000313|EMBL:CBK97525.1, ECO:0000313|Proteomes:UP000008803};
RN [1] {ECO:0000313|EMBL:CBK97525.1, ECO:0000313|Proteomes:UP000008803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70/3 {ECO:0000313|EMBL:CBK97525.1,
RC ECO:0000313|Proteomes:UP000008803};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Eubacterium siraeum 70/3.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK97525.1, ECO:0000313|Proteomes:UP000008803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70/3 {ECO:0000313|EMBL:CBK97525.1,
RC ECO:0000313|Proteomes:UP000008803};
RA Pajon A.;
RL Submitted (MAR-2010) 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; FP929044; CBK97525.1; -; Genomic_DNA.
DR AlphaFoldDB; D4JWQ6; -.
DR KEGG; esu:EUS_25800; -.
DR PATRIC; fig|657319.3.peg.349; -.
DR HOGENOM; CLU_007831_2_2_9; -.
DR Proteomes; UP000008803; 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; 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 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 272..286
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 625 AA; 70247 MW; 96B82056D7057987 CRC64;
MYELDYYDVI VVGAGHAGCE AALAAARLGC KTAVFTLSLD AIANMPCNPC IGGSAKGQLV
RELDSLGGEM GRAADATFIQ SRMLNKGKGP AVHSLRVQSD RVKYHTFMKS VLEHTENLDI
KQAEVTEVCA ENGKITGIKT RLGAFYPAGC VIITTGTYLG GKIHIGELNY QSGPDNVSAA
LQMTESLRNL GLSMRRFKTG TPARVHKRSI DFSVMEEQDG DEYITPFCFD NTFKLENKVK
CYVTYTNAET HRIILDNLDR SPLYAGRIQG VGPRYCPSIE DKIVRFSDKP RHQLFVEPMG
LDTDEYYLQG MSSSLPEDVQ IKFLRTIKGL EHVEIMRPAY AIEYDCCDPL ELYPTLEFKK
ISGLFGAGQF NCTSGYEEAA AQGVIAGMNA AMKIKGREQY ISDRTTSFIG TLIDDLVTKG
CVEPYRMMTS RSEYRLLLRQ DNANDRLVPI GHKFGLISDE RYQRFLERKN ILDNETSRIK
KATIYPCEEL NKMLESKGTS PITQGVKFIE LLKRPQIDYR DLARFDENAP ELEHDIIDKL
EINIKYEGYI KTQTEKIEQM KRLEEKQLPT DIDYKTISGL RLEAQEKLNK HRPLNIGQAG
RISGVNPADV SVLLIWLSGR KHGEN
//
