MNMG_AYWBP
ID MNMG_AYWBP Reviewed; 618 AA.
AC Q2NJ23;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 77.
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=AYWB_453;
OS Aster yellows witches'-broom phytoplasma (strain AYWB).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX NCBI_TaxID=322098;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AYWB;
RX PubMed=16672622; DOI=10.1128/jb.188.10.3682-3696.2006;
RA Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A., Shevchenko D.V.,
RA Tsukerman K., Walunas T., Lapidus A., Campbell J.W., Hogenhout S.A.;
RT "Living with genome instability: the adaptation of phytoplasmas to diverse
RT environments of their insect and plant hosts.";
RL J. Bacteriol. 188:3682-3696(2006).
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 -!- SEQUENCE CAUTION:
CC Sequence=ABC65570.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000061; ABC65570.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041640020.1; NC_007716.1.
DR AlphaFoldDB; Q2NJ23; -.
DR SMR; Q2NJ23; -.
DR STRING; 322098.AYWB_453; -.
DR EnsemblBacteria; ABC65570; ABC65570; AYWB_453.
DR KEGG; ayw:AYWB_453; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_14; -.
DR OrthoDB; 146811at2; -.
DR Proteomes; UP000001934; 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..618
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000345240"
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 268..282
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 365
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 618 AA; 69022 MW; CE6D4B864C57E11C CRC64;
MIYDSIVIGA GHAGIESALI LAKKHNTLLI TGSLKQVASL PCNPSIGGPA KGVVVREIDA
LGGIMAKATD LAQIQIKMLN SSKGPAVRAL RAQIDKLEYP QIILEILQNT PNLTLLEGLV
NNLIIQKNQV QGVCLIDGRK INAKTVIITT GTYLASQILI GDTKKASGPN GVPTTYGIST
QLKEIGFEVI RLKTGTPPRV KKNSIDYSQT KIQMGDNLEQ TFGFLTPQTT KRPQEPCFLT
HTNQTTHQVI RKHLNQSAMY GGYVEGIGPR YCPSIEDKVV RFCDKNSHQI FIEPESLYLN
EMYLQGLSTS MPQHVQHEIL KTIPGLQNAK ITKYAYAIEY DAFNPNQLKH SLETKKIQNL
FLAGQMNGTS GYEEAACQGL MAGINASLKL QNKPPFVLKR NEAYIGVLID DLITKGAKEP
YRLLTSRAEF RLLLRHDNAD LRLKDYGYQL GLIDKKDYNS FQNKKAKINL LLEKSKNYEI
LVNSDNLSYL KQQNSASLGE KTTLAQLIKR PELNFCTLQH FLQEKADKTI YEQVEIQIKY
EGYIAKAQKE AQKLARLEQK KIPSKINYAD IKNLSKEAKE KLDLIKPQTL GQATRILGVN
QVDISILLVY LEKHHALL
