ID A0A1P9X1E8_9BACT Unreviewed; 619 AA.
AC A0A1P9X1E8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=AWR27_20370 {ECO:0000313|EMBL:AQG81459.1};
OS Spirosoma montaniterrae.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=1178516 {ECO:0000313|EMBL:AQG81459.1, ECO:0000313|Proteomes:UP000187941};
RN [1] {ECO:0000313|EMBL:AQG81459.1, ECO:0000313|Proteomes:UP000187941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY10 {ECO:0000313|EMBL:AQG81459.1,
RC ECO:0000313|Proteomes:UP000187941};
RA Oliw E.H.;
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}.
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DR EMBL; CP014263; AQG81459.1; -; Genomic_DNA.
DR RefSeq; WP_077132921.1; NZ_CP014263.1.
DR AlphaFoldDB; A0A1P9X1E8; -.
DR STRING; 1178516.AWR27_20370; -.
DR KEGG; smon:AWR27_20370; -.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000187941; 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 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:UP000187941};
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 11..16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 270..284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 619 AA; 69323 MW; 662750131C9CB3A1 CRC64;
MFSSYDVIVV GAGHAGCEAA HAAATMGSTV LLITMNMQTI AQMSCNPAMG GVAKGQIVRE
VDALGGMSGI ISDKSMIQFR MLNRSKGPAM WSPRCQSDRN MFAWEWRKTL EANKLIDFWQ
DTVNEVLVKD GRITGVKTTL GVTFSAKAVV LTNGTFLNGQ MFIGEKVFGG GRTAERSATG
LTEQLATLGF EAGRMKTGTP PRVDGRSLNY GLMEEQLGDE KPGKFSYTDT PSLTQQRSCW
ITYTNESVHD ELKTGFEKSP MFTGRIKGLG PRYCPSIEDK INRFADKDRH QIFVEPEGWD
TVEVYVNGFS TSLPESVQYD ALRKIPGFEQ VRMFRPGYAV EYDYFPPTQL KSTLETRLIN
NLFFAGQING TTGYEEAACQ GLIAGINAHR NVHEEAEFTI KRSEGYIGVL IDDLITKGTE
EPYRMFTSRA EYRTLLRQDN ADIRLTEKGY AIGLASQERY EKMIQKRDGV ATLTEVIRST
KIKPEDVNNW LLSMNSSPLR EKGSLYTLLK RPEIDQENIY GLLALVPNLP AIGEEVLEQT
IIEIKYEDYL SREKQNAEKL DRWENLTIHP TFDYDRLGAL SFEGREKLKR LRPGTIGQAS
RISGVSPSDV SILLVYMGR
//
