ID A0A0G2J3X8_9SYNE Unreviewed; 348 AA.
AC A0A0G2J3X8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG {ECO:0000256|ARBA:ARBA00020461};
DE AltName: Full=Glucose-inhibited division protein A {ECO:0000256|ARBA:ARBA00031800};
DE Flags: Fragment;
GN ORFNames=TE42_10575 {ECO:0000313|EMBL:KKZ10228.1};
OS Candidatus Synechococcus spongiarum SP3.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1604020 {ECO:0000313|EMBL:KKZ10228.1, ECO:0000313|Proteomes:UP000035067};
RN [1] {ECO:0000313|EMBL:KKZ10228.1, ECO:0000313|Proteomes:UP000035067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP3 {ECO:0000313|EMBL:KKZ10228.1};
RA Burgsdorf I., Slaby B.M., Handley K.M., Haber M., Blom J., Marshall C.W.,
RA Gilbert J.A., Hentschel U., Steindler L.;
RT "Lifestyle Evolution in Cyanobacterial Symbionts of Sponges.";
RL Submitted (JAN-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}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC {ECO:0000256|ARBA:ARBA00025948}.
CC -!- SIMILARITY: Belongs to the MnmG family.
CC {ECO:0000256|ARBA:ARBA00007653}.
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:KKZ10228.1}.
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DR EMBL; JXQG01000108; KKZ10228.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2J3X8; -.
DR Proteomes; UP000035067; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 2.40.30.260; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR002218; MnmG-rel.
DR InterPro; IPR020595; MnmG-rel_CS.
DR InterPro; IPR040131; MnmG_N.
DR PANTHER; PTHR11806; GLUCOSE INHIBITED DIVISION PROTEIN A; 1.
DR PANTHER; PTHR11806:SF0; PROTEIN MTO1 HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF01134; GIDA; 1.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS01280; GIDA_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 10..348
FT /note="MnmG N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01134"
FT NON_TER 348
FT /evidence="ECO:0000313|EMBL:KKZ10228.1"
SQ SEQUENCE 348 AA; 37658 MW; 3BA0EDCDFC6D4D17 CRC64;
MDNFCSERFD VIVVGGGHAG CEAALAAARL GCSTALFTLN LDRIAWQPCN PAVGGPAKSQ
LVHEVDALGG VIGRLADAHA IQKRMLNASR GPAVWALRAQ TDKRRYALGM QRLLQEQPNL
SLREAMVTDL LTTGSRGGGN LRIHGVETYF GSRYGAEAVV LTTGTFLQGR IWIGGRSQSA
GRAGEAAATG LTDALQRLGL EMGRLKTGTP ARVERSSVAL EDLEEQPSDA ADRYFSFDPE
AWISGPQISC HITRTTAATH QLIRDNLHLT PIYGGFLDAK GPRYCPSIED KIVRFAEKES
HQIFLEPEGL DSPELYIQGF STGLPEALQL QLLRTLPGLE HCVMLRPA
//
