MNMG_ECO57
ID MNMG_ECO57 Reviewed; 629 AA.
AC Q8XAY0;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=Z5241, ECs4683;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG58944.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38106.1; -; Genomic_DNA.
DR PIR; C91214; C91214.
DR PIR; D86060; D86060.
DR RefSeq; NP_312710.1; NC_002695.1.
DR RefSeq; WP_000499793.1; NZ_SWKA01000005.1.
DR PDB; 3G05; X-ray; 3.49 A; A/B=2-550.
DR PDBsum; 3G05; -.
DR AlphaFoldDB; Q8XAY0; -.
DR SMR; Q8XAY0; -.
DR STRING; 155864.EDL933_5071; -.
DR EnsemblBacteria; AAG58944; AAG58944; Z5241.
DR EnsemblBacteria; BAB38106; BAB38106; ECs_4683.
DR GeneID; 915333; -.
DR KEGG; ece:Z5241; -.
DR KEGG; ecs:ECs_4683; -.
DR PATRIC; fig|386585.9.peg.4889; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_6; -.
DR OMA; FRPGYAI; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; 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_0000117100"
FT BINDING 13..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 180
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 273..287
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 370
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:3G05"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:3G05"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:3G05"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:3G05"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 78..88
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:3G05"
FT HELIX 101..113
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 134..143
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 145..153
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:3G05"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:3G05"
FT HELIX 249..258
FT /evidence="ECO:0007829|PDB:3G05"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:3G05"
FT HELIX 318..326
FT /evidence="ECO:0007829|PDB:3G05"
FT TURN 329..332
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:3G05"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:3G05"
FT HELIX 369..372
FT /evidence="ECO:0007829|PDB:3G05"
FT HELIX 378..395
FT /evidence="ECO:0007829|PDB:3G05"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:3G05"
FT HELIX 409..416
FT /evidence="ECO:0007829|PDB:3G05"
FT TURN 417..420
FT /evidence="ECO:0007829|PDB:3G05"
FT HELIX 426..432
FT /evidence="ECO:0007829|PDB:3G05"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:3G05"
FT HELIX 444..455
FT /evidence="ECO:0007829|PDB:3G05"
FT HELIX 460..478
FT /evidence="ECO:0007829|PDB:3G05"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:3G05"
FT HELIX 492..496
FT /evidence="ECO:0007829|PDB:3G05"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:3G05"
FT HELIX 509..514
FT /evidence="ECO:0007829|PDB:3G05"
FT HELIX 520..523
FT /evidence="ECO:0007829|PDB:3G05"
FT TURN 527..529
FT /evidence="ECO:0007829|PDB:3G05"
FT HELIX 536..548
FT /evidence="ECO:0007829|PDB:3G05"
SQ SEQUENCE 629 AA; 69565 MW; 194AB2ACCC59F0BA 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 AARLSDDKEG WAPARSQAYL GVLVDDLCTL
GTKEPYRMFT SRAEYRLMLR EDNADLRLTE IGRELGLVDD ERWARFNEKL ENIERERQRL
KSTWVTPSAE AAAEVNAHLT APLSREASGE DLLRRPEMTY EKLTTLTPFA PALTDEQAAE
QVEIQVKYEG YIARQQDEIE KQLRNENTLL PATLDYRQVS GLSNEVIAKL NDHKPASIGQ
ASRISGVTPA AISILLVWLK KQGMLRRSA
