ID B5RL04_BORDL Unreviewed; 626 AA.
AC B5RL04;
DT 04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 96.
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 ECO:0000313|EMBL:ACH93133.1};
GN OrderedLocusNames=BDU_177 {ECO:0000313|EMBL:ACH93133.1};
OS Borrelia duttonii (strain Ly).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borrelia.
OX NCBI_TaxID=412419 {ECO:0000313|EMBL:ACH93133.1, ECO:0000313|Proteomes:UP000000611};
RN [1] {ECO:0000313|EMBL:ACH93133.1, ECO:0000313|Proteomes:UP000000611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ly {ECO:0000313|EMBL:ACH93133.1,
RC ECO:0000313|Proteomes:UP000000611};
RX PubMed=18787695; DOI=10.1371/journal.pgen.1000185;
RA Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J.,
RA Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.;
RT "The genome of Borrelia recurrentis, the agent of deadly louse-borne
RT relapsing fever, is a degraded subset of tick-borne Borrelia duttonii.";
RL PLoS Genet. 4:E1000185-E1000185(2008).
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}.
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DR EMBL; CP000976; ACH93133.1; -; Genomic_DNA.
DR AlphaFoldDB; B5RL04; -.
DR STRING; 412419.BDU_177; -.
DR KEGG; bdu:BDU_177; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_12; -.
DR Proteomes; UP000000611; Chromosome.
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 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 541..611
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT BINDING 15..20
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 276..290
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 626 AA; 70936 MW; B730FB6E4D821D8A CRC64;
MFRKIGMDFD AIVIGGGHAG IEASLALARL NFKTILITQN LDTVGKLSCN PAIGGLAKGN
MVREIDALGG EMGCLIDFSM IQFRILNKSK GPAVQAPRAQ ADKLVYQIKA KETLEMQNNL
ELFQDTVSDF LLNPMKNKIE GVVTERGNKF TSRVVVLTTG TFLRGKIFIG EYKAYMGRIS
EPAAFGLEKI LLELGFEMGR LKTGTPARVH RRSINFAKTE IQFGDSDIIP FSFSNTKIDK
TQLSCYVTYT NKKTHEIISE NMHLSPLYSG EIVGNGPRYC PSIEDKIVKF KDKDKHQIFI
EPEGINTQEM YLNGLSSSLP EDVQKRLINS IDGLEDAVIT RPGYAVEYDY INPIELYASL
ETKRVEGLFV AGQTNGSSGY EEAAAQGLMA GINAALKLQK KDPMILPRTS SYIGVLIDDL
VTKGTKEPYR MFTSRAEHRL NLRHDTSDKR LIKWGYEVGL VSEEKYSRYF FKEKQIEEIK
ELLRHRRLKE KEASSFELKR HINKDFYHIV KDPYINLKDL VNIDPKLNAS KVILEQVELD
IKYEGYINRQ KDLIRKMNNL ELIKLPLDFN YEIDGLSREA REKFVKIQPA NLAQASRVSG
VRNTDIQVLL IYFSNPKNKV VLNLDL
//
