ID A0A133YGK9_9FIRM Unreviewed; 663 AA.
AC A0A133YGK9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=HMPREF1872_00314 {ECO:0000313|EMBL:KXB42334.1};
OS Amygdalobacter nucleatus.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Amygdalobacter.
OX NCBI_TaxID=3029274 {ECO:0000313|EMBL:KXB42334.1, ECO:0000313|Proteomes:UP000070080};
RN [1] {ECO:0000313|Proteomes:UP000070080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA00274 {ECO:0000313|Proteomes:UP000070080};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-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}.
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:KXB42334.1}.
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DR EMBL; LSCV01000003; KXB42334.1; -; Genomic_DNA.
DR RefSeq; WP_066713039.1; NZ_KQ959566.1.
DR AlphaFoldDB; A0A133YGK9; -.
DR STRING; 1497955.HMPREF1872_00314; -.
DR PATRIC; fig|1497955.3.peg.299; -.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000070080; 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 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:UP000070080};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00129}.
FT DOMAIN 578..649
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT BINDING 30..35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 307..321
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 663 AA; 74930 MW; 50BF7380ECE1FB24 CRC64;
MQIQYRDKLE QELSDQKYFI ADKLAVAVVG AGHAGIEAAY AASKIVDKVG LFTLSLDGLA
NMPCNPHIGG TAKGQLVREI DALGGLMGEA ADYNGIHFRM LNLSKGPAVY SPRAQIDRKA
YQRYMKHRLE KVSNIYLKQA EIVDLLWTEV DGQKQILGVI SRYRAVYLAD KVVICSGTYL
SSEIIVGQEK FKQGPDSQAY AEYLSANIAK LGLKMQRFKT GTPVRIHRRS CNFSGMEEQT
GDKQPFCFSF TNTLSYKEPD DTSKAHPLTE PEQQSCFVAY TNEETHEIIR KNIDRSPLFS
GLISGTGTRY CPSIEDKVVK FSDKNRHQLF IEPTGLDTEE LYISGLSSSL PEDVQMQVLH
SIKGLEKAEM TRTAYAIEYD LIDPLELNLT LECKKVNGLY FAGQMNGSSG YEEAACQGLM
AGANAALSYV QAEPLILKRN QAYIGVLIDD LVTKGTAEPY RMMTSRTEYR LSLRQDNADE
RLSDLAYKAH LISQERYELY QKKMAAIKTE LSRLKTVYVT PEQTHIFLAE LNLPDLTQNF
NLYDLFRRPQ FNYATTKAFD TERPDLAPEI MFAVETKHKY AGYIKIEQER IDRFVKLESR
ILPSDIDYTQ LQGLRLEARQ KLQALRPVNL GQASRISGVS PADISVLVVY LETYRREHKQ
AEK
//
