MNMG_RHOPB
ID MNMG_RHOPB Reviewed; 625 AA.
AC Q21CM1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG {ECO:0000255|HAMAP-Rule:MF_00129};
DE AltName: Full=Glucose-inhibited division protein A {ECO:0000255|HAMAP-Rule:MF_00129};
GN Name=mnmG {ECO:0000255|HAMAP-Rule:MF_00129};
GN Synonyms=gidA {ECO:0000255|HAMAP-Rule:MF_00129};
GN OrderedLocusNames=RPC_0290;
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-2006) 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. {ECO:0000255|HAMAP-
CC Rule:MF_00129}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00129};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00129}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00129}.
CC -!- SIMILARITY: Belongs to the MnmG family. {ECO:0000255|HAMAP-
CC Rule:MF_00129}.
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DR EMBL; CP000301; ABD85865.1; -; Genomic_DNA.
DR RefSeq; WP_011470773.1; NC_007925.1.
DR AlphaFoldDB; Q21CM1; -.
DR SMR; Q21CM1; -.
DR STRING; 316056.RPC_0290; -.
DR EnsemblBacteria; ABD85865; ABD85865; RPC_0290.
DR KEGG; rpc:RPC_0290; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_5; -.
DR OMA; FRPGYAI; -.
DR OrthoDB; 146811at2; -.
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; 1.10.150.570; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
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; IPR044920; MnmG_C_subdom.
DR InterPro; IPR040131; MnmG_N.
DR PANTHER; PTHR11806; PTHR11806; 1.
DR PANTHER; PTHR11806:SF0; PTHR11806:SF0; 1.
DR Pfam; PF01134; GIDA; 1.
DR Pfam; PF13932; GIDA_C; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR00136; gidA; 1.
DR PROSITE; PS01280; GIDA_1; 1.
DR PROSITE; PS01281; GIDA_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; NAD; tRNA processing.
FT CHAIN 1..625
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_1000016659"
FT BINDING 11..16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 270..284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 625 AA; 66862 MW; 3E18A4F0249806E5 CRC64;
MQTSFDVIVI GGGHAGCEAA AAAARLGATT ALVTHRFATV GAMSCNPAIG GLGKGHLVRE
VDALDGLMGR VADQGGIQFR MLNRRKGPAV RGPRAQADRK LYAAAMQALI LATPHLSVVE
AEADDLLTSD GRITGIRLAD GRELGAGAVV ITTGTFLRGL IHLGERSWPA GRIDEAPALG
LSKSFERLGF ALGRLKTGTP PRLDGRSIDW GAVEMQPGDE PPEPFSVLTE KITNPQIECG
ITRTTPATHA VIRANVHRSP MYSGQIQSSG PRYCPSIEDK IVRFGDRDGH QIFLEPEGLD
DPTVYPNGIS TSLPEEVQRA ILATIPGLQR TTMLRPGYAI EYDHVDPREL EPTLQAKRLR
GLFLAGQING TTGYEEAAAQ GLVAGLNAAL LASGGGEIAF DRADGYLGVM IDDLVTRGIT
EPYRMFTSRA EYRLTLRADN ADQRLTGQGI ALGCVGAERT EFHTAKMAAL AQAKALAQSL
AITPSQAAKH GLSLNRDGVR RSAFELLAYP EVDWARVEAI WPELAAIEPS IATHLEIDAT
YDVYLKRQTA DVEGFRRDEG LLLTEIDYAL VPGLSNEARG RLEKARPRTV GQAGRLDGLT
PAALGILAAY LRRDQRRKPA GSAAG