MNMG_ONYPE
ID MNMG_ONYPE Reviewed; 617 AA.
AC Q6YQV5;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=PAM_268;
OS Onion yellows phytoplasma (strain OY-M).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX NCBI_TaxID=262768;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY-M;
RX PubMed=14661021; DOI=10.1038/ng1277;
RA Oshima K., Kakizawa S., Nishigawa H., Jung H.-Y., Wei W., Suzuki S.,
RA Arashida R., Nakata D., Miyata S., Ugaki M., Namba S.;
RT "Reductive evolution suggested from the complete genome sequence of a
RT plant-pathogenic phytoplasma.";
RL Nat. Genet. 36:27-29(2004).
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; AP006628; BAD04353.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6YQV5; -.
DR SMR; Q6YQV5; -.
DR STRING; 262768.PAM_268; -.
DR EnsemblBacteria; BAD04353; BAD04353; PAM_268.
DR KEGG; poy:PAM_268; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_14; -.
DR OMA; FRPGYAI; -.
DR OrthoDB; 146811at2; -.
DR BioCyc; OYEL262768:G1G26-325-MON; -.
DR Proteomes; UP000002523; 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..617
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000117144"
FT BINDING 9..14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 120
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 175
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 267..281
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 364
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 617 AA; 68812 MW; B920BFFEB51F5A0A CRC64;
MIYDSIVIGA GHAGVEAALI LAKKHNTLLI TGSLKQVASL PCNPSIGGPA KGVVVREIDA
LGGVMAKAAD LAQIQIKMLN SSKGPAVRAL RAQIDKLEYP QIIFEILQKT LNLTLLEGLV
NNLVIQNNQV QGVCLIDGTK INAKTVIITT GTYLASQILI GDTKKSSGPN GVPTTYGIST
QLKELGFEVI RLKTGTPPRV KKNSIDYSQT KIQMGDNLEQ IFSFVPQTNQ RPQEPCFLTH
TNQTTHQVIQ KHLNQSAMYG GYVEGTGPRY CPSIEDKVVR FCDKNSHQIF IEPESLSLDE
MYLQGLSTSM PQHVQHEILK TIPGLQNAQI TKYAYAIEYD AFNPNQLKHS LETKKIQNLF
LAGQMNGTSG YEEAACQGLM AGINASLKLQ NKPPFVLKRN EAYIGVLIDD LITKGAKEPY
RLLTSRAEFR LLLRHDNADL RLKDYGYQLG LIDEKDYNNF QNKKAKINLL LEKSKNYEIL
VNSDNLSYLK QQKSASLGEK TTLAQLLKRP ELNFCTLQHF LQEKADKTIY EQVEIQIKYE
GYIAKAQKEA QKLARLEQKK IPSKINYADI KNLSKEAQEK LDLIKPQTLG QATRILGVNQ
VDISILLVYL EKHHALL