ID MNMG_AQUAE Reviewed; 617 AA.
AC O66962;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG;
DE AltName: Full=Glucose-inhibited division protein A;
GN Name=mnmG; Synonyms=gidA; OrderedLocusNames=aq_761;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH FAD, AND SUBUNIT.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of gidA from Aquifex aeolicus.";
RL Submitted (JAN-2008) to the PDB data bank.
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:0000250}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MnmG family. {ECO:0000305}.
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DR EMBL; AE000657; AAC06917.1; -; Genomic_DNA.
DR PIR; G70366; G70366.
DR RefSeq; NP_213523.1; NC_000918.1.
DR RefSeq; WP_010880461.1; NC_000918.1.
DR PDB; 2ZXH; X-ray; 3.20 A; A/B=1-617.
DR PDB; 2ZXI; X-ray; 2.30 A; A/B/C/D=1-617.
DR PDBsum; 2ZXH; -.
DR PDBsum; 2ZXI; -.
DR AlphaFoldDB; O66962; -.
DR SMR; O66962; -.
DR DIP; DIP-48311N; -.
DR STRING; 224324.aq_761; -.
DR EnsemblBacteria; AAC06917; AAC06917; aq_761.
DR KEGG; aae:aq_761; -.
DR PATRIC; fig|224324.8.peg.606; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_0; -.
DR InParanoid; O66962; -.
DR OrthoDB; 9815560at2; -.
DR EvolutionaryTrace; O66962; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
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; PR00368; FADPNR.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; FAD; Flavoprotein; NAD; Reference proteome;
KW tRNA processing.
FT CHAIN 1..617
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000117046"
FT BINDING 14..19
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 126
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 181
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 280..294
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 377
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|Ref.2"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 126..141
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 184..190
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 256..264
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:2ZXH"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:2ZXH"
FT HELIX 287..293
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 325..332
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 348..354
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 364..370
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 376..379
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 384..402
FT /evidence="ECO:0007829|PDB:2ZXI"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 416..427
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:2ZXI"
FT TURN 441..445
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 451..461
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:2ZXH"
FT HELIX 467..487
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 491..496
FT /evidence="ECO:0007829|PDB:2ZXI"
FT STRAND 499..504
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 505..508
FT /evidence="ECO:0007829|PDB:2ZXI"
FT TURN 509..512
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 515..522
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 530..552
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 554..560
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 570..572
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 578..587
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 592..595
FT /evidence="ECO:0007829|PDB:2ZXI"
FT HELIX 603..612
FT /evidence="ECO:0007829|PDB:2ZXI"
SQ SEQUENCE 617 AA; 69644 MW; 1DAB1BDFEFCBA6DD CRC64;
MAWVVDEFDV VVIGGGHAGI EAALAAARMG AKTAMFVLNA DTIGQMSCNP AIGGIAKGIV
VREIDALGGE MGKAIDQTGI QFKMLNTRKG KAVQSPRAQA DKKRYREYMK KVCENQENLY
IKQEEVVDII VKNNQVVGVR TNLGVEYKTK AVVVTTGTFL NGVIYIGDKM IPGGRLGEPR
SEGLSDFYRR FDFPLIRFKT GTPARLDKRT IDFSALEVAP GDDPPPKFSF WTEPVGSYWF
PKGKEQVNCW ITYTTPKTHE IIRKNLHRTA LYGGLIKGIG PRYCPSIEDK IVKFPDKERH
QIFLEPEGLD TIEIYPNGLS TSLPEEVQWE MYRSIPGLEN VVLIRPAYAI EYDVVPPTEL
YPTLETKKIR GLFHAGNFNG TTGYEEAAGQ GIVAGINAAL RAFGKEPIYL RRDESYIGVM
IDDLTTKGVT EPYRLFTSRS EYRLYIRQDN AILRLAKLGR ELGLLSEEQY KLVKELEREI
EKWKEFYKSE RVSVAVGGDT RSYSVATLMT MNYTLDDVKE KFGYEVPQHP YVKEEVEIQL
KYEPYIERER KLNEKLKKLE DTKIPPDIDY DKIPGLTKEA REKLKKFKPI TVGQASRIDG
ITPAAITALL VYLGKLD
//
