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Database: UniProt
Entry: A0A370K4H9_9GAMM
LinkDB: A0A370K4H9_9GAMM
Original site: A0A370K4H9_9GAMM 
ID   A0A370K4H9_9GAMM        Unreviewed;       625 AA.
AC   A0A370K4H9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=DVT68_19610 {ECO:0000313|EMBL:RDI96930.1};
OS   Dyella solisilvae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dyella.
OX   NCBI_TaxID=1920168 {ECO:0000313|EMBL:RDI96930.1, ECO:0000313|Proteomes:UP000254711};
RN   [1] {ECO:0000313|EMBL:RDI96930.1, ECO:0000313|Proteomes:UP000254711}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DHG54 {ECO:0000313|EMBL:RDI96930.1,
RC   ECO:0000313|Proteomes:UP000254711};
RA   Gao Z., Qiu L.;
RT   "Dyella solisilvae sp. nov., isolated from the pine and broad-leaved mixed
RT   forest soil.";
RL   Submitted (JUL-2018) 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:RDI96930.1}.
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DR   EMBL; QQSY01000009; RDI96930.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A370K4H9; -.
DR   OrthoDB; 9815560at2; -.
DR   Proteomes; UP000254711; 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   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   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          546..617
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme C-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01228"
FT   BINDING         13..18
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT   BINDING         273..287
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   625 AA;  68193 MW;  000A58CE68CBAAE4 CRC64;
     MFHPTPYDVI VIGGGHAGTE AALASARTGA RTLLLSHNIE TIGQMSCNPA IGGIGKGHLV
     KEIDALGGAM AHAADLAGIQ WRTLNASKGP AVRATRCQAD RALYKAAIRR IVETQPQLEL
     FQQAVDDLIL EGGRVTGVVT QMGLKFQARA VVLTAGTFLA GKIHIGQAQY AGGRAGDPPA
     STLAQKLREL PVAADRLKTG TPPRIDLRSI DFTGLEEQPG DDPAPVFSYL GSRDEHPRQV
     SCWITHTSEH THELIRGALD RSPLYSGQIE GIGPRYCPSI EDKVVRFAEK SSHQIFIEPE
     GLDTFEVYPN GISTSLPYDV QLALVRSIKG FEHAHITRPG YAIEYDYFDP RGLHPWLETK
     TIPGLYFAGQ INGTTGYEEA GAQGLIAGLN AALAVKGEAP WYPRRDEAYI GVLIDDLTSN
     GTIEPYRMFT SRAEYRLHLR EDNADLRLTE TGHRLGVVPQ ARYDALRAKR DAVAQETQRL
     GAIWAAPSNG LGANVERQLG ITLSRETNAL DLLRRPELDY AKLTSVEGIG PAVSDDDVAA
     QVEVQTKYAG YLDRQREEIE RQRRHEQTAI PNGFDYDKVR GLSAEVLLKL KRVQPETIGQ
     AARISGVTPA AISLLLVHLK RRDAA
//
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