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Database: UniProt
Entry: A0A0R2XSD6_9BACT
LinkDB: A0A0R2XSD6_9BACT
Original site: A0A0R2XSD6_9BACT 
ID   A0A0R2XSD6_9BACT        Unreviewed;       646 AA.
AC   A0A0R2XSD6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=ABS34_03460 {ECO:0000313|EMBL:KRP37281.1};
OS   Opitutaceae bacterium BACL24 MAG-120322-bin51.
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX   NCBI_TaxID=1655636 {ECO:0000313|EMBL:KRP37281.1, ECO:0000313|Proteomes:UP000054041};
RN   [1] {ECO:0000313|EMBL:KRP37281.1, ECO:0000313|Proteomes:UP000054041}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BACL24 MAG-120322-bin51 {ECO:0000313|EMBL:KRP37281.1};
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, 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:KRP37281.1}.
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DR   EMBL; LIDO01000024; KRP37281.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2XSD6; -.
DR   Proteomes; UP000054041; 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; 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   PANTHER; PTHR11806; GLUCOSE INHIBITED DIVISION PROTEIN A; 1.
DR   PANTHER; PTHR11806:SF0; PROTEIN MTO1 HOMOLOG, MITOCHONDRIAL; 1.
DR   Pfam; PF01134; GIDA; 2.
DR   Pfam; PF13932; GIDA_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
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   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00129}.
FT   DOMAIN          563..634
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme C-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01228"
FT   BINDING         19..24
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT   BINDING         314..328
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   646 AA;  72113 MW;  B902044B57089A1F CRC64;
     MSGGLKFGPN QPYDVIVCGA GHAGCEAALA AARLGADVLM LTGNLDTVAQ MSCNPAIGGQ
     AKGHMVREID ALGGEMAINA DTTAIQFRLL NASKGPAVQA PRAQCDKKAY QYRMKHVLEL
     QANLDLFQAM VQRLIYKDGR VVGVKTNLDV DFYAKTVVVT TGTFLRGLMH VGKNTNKGGR
     MGDFSAEGLS GSFLEAGIEL ERLKTGTPAR ILGSSIDFSQ LEEQQGDPEP TLFAFYDTRG
     VDNVFHVEQS EQGARESEHE LFHVEHPGQR KLGWLPGKDQ VSCWMTYTGA ETRQVVTDNL
     HLSPMYSGQI EGTGPRYCPS IEDKFVRFAD KERHMLFLEP EGRNTNEWYI NGLSTSLPFS
     VQLDMLRSID GLEKVHMLRP AYAVEYDFAP PTQLFPTLES KKVENLFFAG QINGTSGYEE
     AAGQGLIAGV NAVQKLRGSE PLVLKRHEAY LGVLIDDLVT KGTKEPYRMF SSRAEHRLLF
     NHPSAEIRLL EHSSRLQLVD SKRLKRIEVK AAKVAEWTQR LEDELRAGES YALHLRRSHS
     QDDFPQELKA ESKEVRAEVH YRVVFKGYLE RERKQIEKMK HIDHIRIPDG FDYSLVKGLR
     TESAQKLIEI MPRTLGQANR ISGVNPADIS ILMVNLEARR ANKKKA
//
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