ID A0A0G0AZ38_9BACT Unreviewed; 618 AA.
AC A0A0G0AZ38;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 33.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG {ECO:0000256|HAMAP-Rule:MF_00129};
DE AltName: Full=Glucose-inhibited division protein A {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=SZ59_C0002G0063 {ECO:0000313|EMBL:KKP24217.1};
OS candidate division TM6 bacterium GW2011_GWF2_28_16.
OC Bacteria; Candidatus Dependentiae.
OX NCBI_TaxID=1619077 {ECO:0000313|EMBL:KKP24217.1, ECO:0000313|Proteomes:UP000033842};
RN [1] {ECO:0000313|EMBL:KKP24217.1, ECO:0000313|Proteomes:UP000033842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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|HAMAP-
CC 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:KKP24217.1}.
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DR EMBL; LBNX01000002; KKP24217.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0AZ38; -.
DR PATRIC; fig|1619077.4.peg.273; -.
DR Proteomes; UP000033842; 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 HAMAP; MF_00129; MnmG_GidA; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR004416; MnmG.
DR InterPro; IPR002218; MnmG-rel.
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 PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM01228; GIDA_assoc_3; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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 536..607
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"
SQ SEQUENCE 618 AA; 69601 MW; A61FC87576DA89A6 CRC64;
MNNKFDVIVV GAGHAGVEAA YAAAKMGSKT LLITLDKNKM ALMPCNPSIG GLGKGHIVYE
ISALGGMMPK LCTHSYLQAR MLNTSKGPAV QGLRLQIHKF EYAKKARELL EQVENLNIHE
GMVIQVITNN NKITGVRTQA NQEFYAPAVI ITSGTFLNGV THIGFETQSA GRRGELAVPT
LTKSLELATG IKFKRLKTGT PPRLLKSSID FSVLEKQEAS KLEYLYEFDP INIQEKESCY
ITTTNENTHK IIRENLERSA LYGGKISGIG PRYCPSIEDK IKRHPDRNSH HVFVEPDGEN
LEKIYPAGIS TSLPLNVQEQ YVRSIKGFEK AIFTDPGYAI EYDFIEPHNL KYTLESKTVS
GLYFAGQVIG TTGYEEAAGL GLVAGINAHL KIHNQEPFIL SRTESYIGVM IDDLITIGID
EPYRMFTSRA ERRLLLRQDN VFLRLMPYGK KFNLIDNKLY NKFLREKEII ENSINLINNL
GTQSDIFKLF HDINWEKETQ IKAQENLLNL YNKKINNKIN IQELTSRILL CIHAQVRYAG
YIEKEKAETE KLLKFQALKI PKEINYSQMP GLSVELQNKL KKHSPSTIAQ AQLIPGMTPA
AISILIFQSR VLERQVKQ
//
