MNMG_PROM1
ID MNMG_PROM1 Reviewed; 656 AA.
AC A2C5E1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=NATL1_21451;
OS Prochlorococcus marinus (strain NATL1A).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167555;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL1A;
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; CP000553; ABM76701.1; -; Genomic_DNA.
DR RefSeq; WP_011824639.1; NC_008819.1.
DR AlphaFoldDB; A2C5E1; -.
DR SMR; A2C5E1; -.
DR STRING; 167555.NATL1_21451; -.
DR PRIDE; A2C5E1; -.
DR EnsemblBacteria; ABM76701; ABM76701; NATL1_21451.
DR KEGG; pme:NATL1_21451; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_3; -.
DR OMA; FRPGYAI; -.
DR Proteomes; UP000002592; 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; tRNA processing.
FT CHAIN 1..656
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_1000016636"
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; 73283 MW; 56EFCD6668278BF2 CRC64;
MITKQSSNES FDVIVVGGGH AGCEAALTSA RLGLNTALFT LNLDRIAWQP CNPAVGGPAK
SQLVHEVDAL GGIIGKLADL TALQKRVLNA SRGPAVRALR AQTDKRSYAH EMLKILQNTP
NLKIREAMVT GLEIEHYPNQ IDQKTPEIQE RIGFIKGIKT YFGSVFHAKA VVLTTGTFLG
GRIWIGNQSM SAGRAGEQAS EGLTEELKKL GFTTDRLKTG TPARVDRRTI DLDSLDEQLS
DASDKFFSFD PLSWKSGEQM SCHITRTTKE THQLIKNNLH LTPIYGGFID SKGPRYCPSI
EDKIVRFADK DSHQIFLEPE GRDTPEMYVQ GFSTGLPENL QLELLRTLPG LQNCVMLRPA
YAVEYDYIPA TQLEATLETK RISGLYSAGQ LNGTTGYEEA AAQGLVAGLN AARLVNNKEG
IIFERESSYI GTMIDDLVTK DLKEPYRVLT SRSEYRLILR GDNADRRLTP LGYQLGLIDE
RRWNIFNAKQ QLINQEKERL DKERIKESDK CAKEIFSSTG TPIKGSLTLA NFLRRTNIHY
KDLITYNLTT QSIPLDVEEA VEIDIKYSGY LERQKAQINQ LKQQSKKLLP KNLNYNNIET
LSKEAREKLT ISQPKSLGHA AQVPGVSKAD LTALLVWLKI EKMKKVKRKD SLQITN