MNMG_ECOLI
ID MNMG_ECOLI Reviewed; 629 AA.
AC P0A6U3; P03816; P17112; Q2M859;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG;
DE AltName: Full=Glucose-inhibited division protein A;
GN Name=mnmG; Synonyms=gidA, trmF; OrderedLocusNames=b3741, JW3719;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6395859; DOI=10.1042/bj2240799;
RA Walker J.E., Gay N.J., Saraste M., Eberle A.N.;
RT "DNA sequence around the Escherichia coli unc operon. Completion of the
RT sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and
RT phoS.";
RL Biochem. J. 224:799-815(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 515.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-196.
RX PubMed=6357950; DOI=10.1016/0378-1119(83)90087-2;
RA Buhk H.-J., Messer W.;
RT "The replication origin region of Escherichia coli: nucleotide sequence and
RT functional units.";
RL Gene 24:265-279(1983).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
RC STRAIN=K12;
RX PubMed=370832; DOI=10.1073/pnas.76.2.575;
RA Sugimoto K., Oka A., Sugisaki H., Takanami M., Nishimura A., Yasuda Y.,
RA Hirota Y.;
RT "Nucleotide sequence of Escherichia coli K-12 replication origin.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:575-579(1979).
RN [7]
RP FUNCTION.
RX PubMed=9603884; DOI=10.1128/jb.180.11.2931-2935.1998;
RA Nakayashiki T., Inokuchi H.;
RT "Novel temperature-sensitive mutants of Escherichia coli that are unable to
RT grow in the absence of wild-type tRNA6Leu.";
RL J. Bacteriol. 180:2931-2935(1998).
RN [8]
RP FUNCTION.
RX PubMed=11544186; DOI=10.1101/gad.207701;
RA Bregeon D., Colot V., Radman M., Taddei F.;
RT "Translational misreading: a tRNA modification counteracts a +2 ribosomal
RT frameshift.";
RL Genes Dev. 15:2295-2306(2001).
RN [9]
RP FUNCTION, COFACTOR, INTERACTION WITH MNME, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF GLY-13 AND GLY-15.
RC STRAIN=K12;
RX PubMed=17062623; DOI=10.1093/nar/gkl752;
RA Yim L., Moukadiri I., Bjoerk G.R., Armengod M.-E.;
RT "Further insights into the tRNA modification process controlled by proteins
RT MnmE and GidA of Escherichia coli.";
RL Nucleic Acids Res. 34:5892-5905(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), SUBUNIT, AND NAD AND FAD BINDING.
RX PubMed=18565343; DOI=10.1016/j.jmb.2008.04.072;
RA Meyer S., Scrima A., Versees W., Wittinghofer A.;
RT "Crystal structures of the conserved tRNA-modifying enzyme GidA:
RT implications for its interaction with MnmE and substrate.";
RL J. Mol. Biol. 380:532-547(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:0000269|PubMed:11544186, ECO:0000269|PubMed:17062623,
CC ECO:0000269|PubMed:9603884}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:17062623};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC {ECO:0000269|PubMed:18565343}.
CC -!- INTERACTION:
CC P0A6U3; P25522: mnmE; NbExp=6; IntAct=EBI-550977, EBI-550986;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17062623}.
CC -!- SIMILARITY: Belongs to the MnmG family. {ECO:0000305}.
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DR EMBL; X01631; CAA25773.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62093.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76764.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77547.1; -; Genomic_DNA.
DR EMBL; K00826; AAA24250.2; -; Genomic_DNA.
DR EMBL; J01657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; F65177; BVECQA.
DR RefSeq; NP_418197.1; NC_000913.3.
DR RefSeq; WP_000499788.1; NZ_STEB01000015.1.
DR PDB; 3CES; X-ray; 2.41 A; A/B/C/D=1-629.
DR PDB; 3CP2; X-ray; 2.90 A; A=1-629.
DR PDBsum; 3CES; -.
DR PDBsum; 3CP2; -.
DR AlphaFoldDB; P0A6U3; -.
DR SMR; P0A6U3; -.
DR BioGRID; 4263258; 181.
DR BioGRID; 852550; 1.
DR ComplexPortal; CPX-5361; tRNA uridine 5-carboxymethylaminomethyl modification complex.
DR DIP; DIP-35786N; -.
DR IntAct; P0A6U3; 12.
DR STRING; 511145.b3741; -.
DR jPOST; P0A6U3; -.
DR PaxDb; P0A6U3; -.
DR PRIDE; P0A6U3; -.
DR EnsemblBacteria; AAC76764; AAC76764; b3741.
DR EnsemblBacteria; BAE77547; BAE77547; BAE77547.
DR GeneID; 66672355; -.
DR GeneID; 948248; -.
DR KEGG; ecj:JW3719; -.
DR KEGG; eco:b3741; -.
DR PATRIC; fig|1411691.4.peg.2959; -.
DR EchoBASE; EB0370; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_6; -.
DR InParanoid; P0A6U3; -.
DR OMA; FRPGYAI; -.
DR PhylomeDB; P0A6U3; -.
DR BioCyc; EcoCyc:EG10375-MON; -.
DR BioCyc; MetaCyc:EG10375-MON; -.
DR EvolutionaryTrace; P0A6U3; -.
DR PRO; PR:P0A6U3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0002144; C:cytosolic tRNA wobble base thiouridylase complex; IPI:ComplexPortal.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
DR GO; GO:0140018; P:regulation of cytoplasmic translational fidelity; IC:ComplexPortal.
DR GO; GO:0009411; P:response to UV; IMP:EcoCyc.
DR GO; GO:0030488; P:tRNA methylation; IMP:EcoCyc.
DR GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; IDA:ComplexPortal.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; FAD; Flavoprotein; NAD; Reference proteome;
KW tRNA processing.
FT CHAIN 1..629
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000117099"
FT BINDING 13..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 273..287
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 370
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MUTAGEN 13
FT /note="G->A: Decrease in FAD binding and partial loss of
FT activity. Loss of activity; when associated with A-15."
FT /evidence="ECO:0000269|PubMed:17062623"
FT MUTAGEN 15
FT /note="G->A: Decrease in FAD binding and partial loss of
FT activity. Loss of activity; when associated with A-13."
FT /evidence="ECO:0000269|PubMed:17062623"
FT CONFLICT 515
FT /note="Missing (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:3CES"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:3CES"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:3CES"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:3CES"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:3CP2"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:3CES"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 101..113
FT /evidence="ECO:0007829|PDB:3CES"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:3CES"
FT STRAND 125..140
FT /evidence="ECO:0007829|PDB:3CES"
FT STRAND 143..153
FT /evidence="ECO:0007829|PDB:3CES"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:3CES"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:3CES"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:3CES"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:3CES"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:3CES"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:3CES"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:3CP2"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:3CES"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 258..261
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 280..286
FT /evidence="ECO:0007829|PDB:3CES"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:3CES"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:3CES"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 318..326
FT /evidence="ECO:0007829|PDB:3CES"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:3CES"
FT STRAND 341..348
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:3CES"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:3CES"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 377..395
FT /evidence="ECO:0007829|PDB:3CES"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 409..420
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 429..433
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 434..438
FT /evidence="ECO:0007829|PDB:3CP2"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 444..455
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 460..481
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 492..496
FT /evidence="ECO:0007829|PDB:3CES"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 509..513
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 520..523
FT /evidence="ECO:0007829|PDB:3CES"
FT TURN 527..529
FT /evidence="ECO:0007829|PDB:3CES"
FT HELIX 536..547
FT /evidence="ECO:0007829|PDB:3CES"
FT TURN 549..552
FT /evidence="ECO:0007829|PDB:3CP2"
SQ SEQUENCE 629 AA; 69521 MW; 54FD79807E901724 CRC64;
MFYPDPFDVI IIGGGHAGTE AAMAAARMGQ QTLLLTHNID TLGQMSCNPA IGGIGKGHLV
KEVDALGGLM AKAIDQAGIQ FRILNASKGP AVRATRAQAD RVLYRQAVRT ALENQPNLMI
FQQAVEDLIV ENDRVVGAVT QMGLKFRAKA VVLTVGTFLD GKIHIGLDNY SGGRAGDPPS
IPLSRRLREL PLRVGRLKTG TPPRIDARTI DFSVLAQQHG DNPMPVFSFM GNASQHPQQV
PCYITHTNEK THDVIRSNLD RSPMYAGVIE GVGPRYCPSI EDKVMRFADR NQHQIFLEPE
GLTSNEIYPN GISTSLPFDV QMQIVRSMQG MENAKIVRPG YAIEYDFFDP RDLKPTLESK
FIQGLFFAGQ INGTTGYEEA AAQGLLAGLN AARLSADKEG WAPARSQAYL GVLVDDLCTL
GTKEPYRMFT SRAEYRLMLR EDNADLRLTE IGRELGLVDD ERWARFNEKL ENIERERQRL
KSTWVTPSAE AAAEVNAHLT APLSREASGE DLLRRPEMTY EKLTTLTPFA PALTDEQAAE
QVEIQVKYEG YIARQQDEIE KQLRNENTLL PATLDYRQVS GLSNEVIAKL NDHKPASIGQ
ASRISGVTPA AISILLVWLK KQGMLRRSA
