MNMG_CHLTE
ID MNMG_CHLTE Reviewed; 621 AA.
AC Q8KA85;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG;
DE AltName: Full=Glucose-inhibited division protein A;
GN Name=mnmG; Synonyms=gidA; OrderedLocusNames=CT2283;
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=194439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH FAD, AND SUBUNIT.
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. {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; AE006470; AAM73496.1; -; Genomic_DNA.
DR RefSeq; NP_663154.1; NC_002932.3.
DR RefSeq; WP_010933931.1; NC_002932.3.
DR PDB; 3CP8; X-ray; 3.20 A; A/B/C/D=1-621.
DR PDBsum; 3CP8; -.
DR AlphaFoldDB; Q8KA85; -.
DR SMR; Q8KA85; -.
DR STRING; 194439.CT2283; -.
DR EnsemblBacteria; AAM73496; AAM73496; CT2283.
DR KEGG; cte:CT2283; -.
DR PATRIC; fig|194439.7.peg.2076; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_10; -.
DR OMA; FRPGYAI; -.
DR OrthoDB; 146811at2; -.
DR EvolutionaryTrace; Q8KA85; -.
DR Proteomes; UP000001007; 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..621
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000117086"
FT BINDING 8..13
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18565343"
FT BINDING 120
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18565343"
FT BINDING 269..283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 366
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18565343"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 49..61
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:3CP8"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 96..108
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 140..148
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 179..185
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:3CP8"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 245..252
FT /evidence="ECO:0007829|PDB:3CP8"
FT TURN 253..257
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 277..282
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 314..321
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 337..344
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 353..359
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 373..392
FT /evidence="ECO:0007829|PDB:3CP8"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 405..415
FT /evidence="ECO:0007829|PDB:3CP8"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 440..450
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 456..478
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 483..493
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 505..508
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 509..512
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 515..519
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 523..528
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 531..534
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 536..547
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 549..565
FT /evidence="ECO:0007829|PDB:3CP8"
FT STRAND 572..574
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 586..593
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 598..601
FT /evidence="ECO:0007829|PDB:3CP8"
FT HELIX 609..616
FT /evidence="ECO:0007829|PDB:3CP8"
SQ SEQUENCE 621 AA; 68097 MW; 752ED5CA7F9A38BF CRC64;
MYDVIVVGAG HAGCEAALAV ARGGLHCLLI TSDLSAVARM SCNPAIGGVA KGQITREIDA
LGGEMGKAID ATGIQFRMLN RSKGPAMHSP RAQADKTQYS LYMRRIVEHE PNIDLLQDTV
IGVSANSGKF SSVTVRSGRA IQAKAAILAC GTFLNGLIHI GMDHFPGGRS TAEPPVEGLT
ESLASLGFSF GRLKTGTPPR IDSRSVDYTI VTEQPGDVDP VPFSFSSTSV ANRNLVSCYL
TKTTEKTHDI LRTGFDRSPL FTGKVQGVGP RYCPSIEDKI SRFPDKSSHH IFLEPEGTDT
VEMYVNGFST SLPEDIQIAG LRSIPGLEEA KMIRPGYAIE YDFFHPWQIR STMETRPVEN
LFFAGQINGT SGYEEAAAQG LMAGINAVRK ILGKELIVLG RDQAYIGVLI DDLITKETKE
PYRMFTSSAE HRLILRHDNA DLRLRKIGYD CNLVSSDDLH RTESIIKRVQ HCLEVMKTAK
VTPAEINTLL MNKGLQELKT PARALSLIKR PGISLQDILE HSLSVRSAAE ELCNDPRVAE
QVQIEIKYEG YIKREQLVAD RIARLDSLHI PDNFNYDSLN SLSSEGREKL LKHRPATIGQ
ASRILGVSPS DVSILMIRLG R
