MNMG_PORGI
ID MNMG_PORGI Reviewed; 625 AA.
AC Q7MTG9;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
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}; OrderedLocusNames=PG_1992;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE015924; AAQ66963.1; -; Genomic_DNA.
DR RefSeq; WP_005874915.1; NC_002950.2.
DR AlphaFoldDB; Q7MTG9; -.
DR SMR; Q7MTG9; -.
DR STRING; 242619.PG_1992; -.
DR EnsemblBacteria; AAQ66963; AAQ66963; PG_1992.
DR KEGG; pgi:PG_1992; -.
DR PATRIC; fig|242619.8.peg.1847; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_10; -.
DR OMA; FRPGYAI; -.
DR OrthoDB; 146811at2; -.
DR BioCyc; PGIN242619:G1G02-1864-MON; -.
DR Proteomes; UP000000588; 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..625
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000117149"
FT BINDING 11..16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 271..285
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 625 AA; 69968 MW; 2D23334FF43CA7B2 CRC64;
MQFNYDVIVV GAGHAGCEAA AAAAKLGSQV LLITPDMNKI AQMSCNPAVG GIAKGQIVRE
IDALGGRMGI VTDATAIQFR MLNRSKGPAM WSPRAQSDRM RFMEAWRDIV EHEPNLYMWQ
DSVRCLSIRQ GAVAGVVTAL GVEFQARTVV LTTGTFLGGV MHFGERMIEG GRIAEPAFHG
ITEQLRDLGF RTDRMKTGTP ARIDGRSIDF SLTTEQSGEE DHHRFSYMDT PRRVLRQRSC
YALYTNPECH EILSKGLDRS PLYNGQIQSI GPRYCPSIET KIVTFADKEM HQLFLEPEGE
TSNEFYLNGF SSSLPLEIQL EALKAIPALR HVHIYRPGYA IEYDFFDPTQ LRHTLETKPV
KGLFFAGQIN GTTGYEEAAG QGLIAGINAH LHCHGAGEFT LGRDEAYIGV LIDDLVSKGV
DEPYRMFTSR AEYRILLRQD DADMRLTPKA EAIGLADSRR SELLREKQVF RDKLIDFTHK
FSLKPDLINP HLESAGHLPL KQGIKLYDLL LRPQIGMNEV CSMVPSLQRI VEEIPASRRE
EIVEAAEILI KYDGYIKRER ALADKINRLE SIRLPQHVDY MQMQSLSTEA RQKLTSIRPE
TIAQASRIPG VSPHDVSILL VLCGR