ID A0A0R2UZ82_9PROT Unreviewed; 410 AA.
AC A0A0R2UZ82;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=ABS16_06255 {ECO:0000313|EMBL:KRP04233.1};
OS Pelagibacteraceae bacterium BACL20 MAG-120920-bin64.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae.
OX NCBI_TaxID=1655618 {ECO:0000313|EMBL:KRP04233.1, ECO:0000313|Proteomes:UP000050912};
RN [1] {ECO:0000313|EMBL:KRP04233.1, ECO:0000313|Proteomes:UP000050912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL1 MAG-120920-bin64 {ECO:0000313|EMBL:KRP04233.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-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:KRP04233.1}.
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DR EMBL; LICT01000387; KRP04233.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2UZ82; -.
DR Proteomes; UP000050912; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR004416; MnmG.
DR InterPro; IPR002218; MnmG-rel.
DR InterPro; IPR020595; MnmG-rel_CS.
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 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 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 1..307
FT /note="MnmG N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01134"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRP04233.1"
FT NON_TER 410
FT /evidence="ECO:0000313|EMBL:KRP04233.1"
SQ SEQUENCE 410 AA; 46706 MW; E924D88A023A0EBD CRC64;
AVQGPRTQSD RSLYRKYMQE KLLNYCNLSI FPDPVIKFIF DKNTISGFET KSGKRILCSK
LILTTGTFLN GLIHIGDERT PAGRFDEKPS TGLSEQLEKY DFKIGRLKTG TPPRLDSRTI
KYDNLEEQFA DEDPYFFSFL TKKNLNKQVS CRMTYTNEKV HKIIQKNIKR SAMYSGSIQG
VGPRYCPSIE DKIVKFADKD RHQIYLEPEG LNDHTIYPNG ISTSLPFDVQ QEICNNINGL
ENVKIIRPGY AIEYDYIDPR ELFLTLETKK IQNLYLAGQI NGTTGYEEAA AQGLIAGINA
ALSFKKEEPF ILDRSDAYIG VMIDDLVTKG VAEPYRMFTS RAEYRLSLRA DNADQRLTNK
GINIGLISKI REDIFIDKEY KLGIVSKRMS ELSISPNKIK DFDIKIAKDG
//
