MNMG_PROMT
ID MNMG_PROMT Reviewed; 656 AA.
AC Q46IB4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=PMN2A_1274;
OS Prochlorococcus marinus (strain NATL2A).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59920;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL2A;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000095; AAZ58764.1; -; Genomic_DNA.
DR RefSeq; WP_011295618.1; NC_007335.2.
DR AlphaFoldDB; Q46IB4; -.
DR SMR; Q46IB4; -.
DR STRING; 59920.PMN2A_1274; -.
DR EnsemblBacteria; AAZ58764; AAZ58764; PMN2A_1274.
DR KEGG; pmn:PMN2A_1274; -.
DR HOGENOM; CLU_007831_2_2_3; -.
DR OMA; FRPGYAI; -.
DR OrthoDB; 146811at2; -.
DR PhylomeDB; Q46IB4; -.
DR Proteomes; UP000002535; 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 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; NAD; Reference proteome; tRNA processing.
FT CHAIN 1..656
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_1000016640"
FT BINDING 17..22
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 129
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 200
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 293..307
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 390
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 656 AA; 73280 MW; 4C8494871CA5815E CRC64;
MITKQSSNES FDVIVVGGGH AGCEAALTSA RLGLNTALFT LNLDRIAWQP CNPAVGGPAK
SQLVHEVDAL GGIIGKLADL TALQKRVLNA SRGPAVRALR AQTDKRSYAH EMLKILQNTP
NLKIREAMVT GLEVEHYPNQ IDQKTPEIQE RIGFIKGIKT YFGSVFHAKA VVLTTGTFLG
GRIWIGNQSM SAGRAGEQAS EGLTEELKKL GFTTDRLKTG TPARVDRRTI DLDSLDEQLS
DASDKFFSFD PLSWKSGEQM SCHITRTTKQ THQLIKNNLH LTPIYGGFID SKGPRYCPSI
EDKIVRFADK DSHQIFLEPE GRDTPEMYVQ GFSTGLPENL QLELLRTLPG LQNCVMLRPA
YAVEYDYIPA TQLEATLETK RISGLYSAGQ LNGTTGYEEA AAQGLVAGLN AARLVNNKEG
IIFERESSYI GTMIDDLVTK DLKEPYRVLT SRSEYRLILR GDNADRRLTP LGYQLGLIDE
RRWKIFNAKQ QLINQEKERL EKERIKESDK SAKEIYSSTG TPIKGSLTLA NFLRRTNIHY
KDLITFNLTT QSIPLDVEEG VEIDIKYSGY LERQKAQINQ LKQQSKKLLP KNLNYNNIET
LSKEAREKLT ISQPKSLGHA AQLPGVSKAD LTALLVWLKI EKMKKVKRKD SLQITN
