ID   MNMG_PSYWF              Reviewed;         642 AA.
AC   A5WGD0;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
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=PsycPRwf_1781;
OS   Psychrobacter sp. (strain PRwf-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=349106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRwf-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter sp. PRwf-1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000713; ABQ94721.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5WGD0; -.
DR   SMR; A5WGD0; -.
DR   STRING; 349106.PsycPRwf_1781; -.
DR   EnsemblBacteria; ABQ94721; ABQ94721; PsycPRwf_1781.
DR   KEGG; prw:PsycPRwf_1781; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_6; -.
DR   OMA; FRPGYAI; -.
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.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; NAD; tRNA processing.
FT   CHAIN           1..642
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345320"
FT   BINDING         24..29
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         284..298
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   642 AA;  70120 MW;  FD3375A8B6B52F20 CRC64;
     MSSTSTSNTA GITYPKAYDV VVIGGGHAGT EAALAAARMG AQTLLLTHNI ETLGQMSCNP
     AIGGIGKSHL VREIDALGGA MALATDKAGI QFRVLNSRKG AAVRATRAQA DRILYKAAIR
     HTLENQPNLD LFQQGADDIL VENGKACAVV TATGIIFRTK TVVLTSGTFL GGVIHIGLDN
     SKGGRAGDQP SIKLAERLRE LKLPVGRLKT GTPARIDART VDFSVMQTQP GDTPLPVMSF
     MGNVDMHPEQ VNCFITHTNE KTHDIIRKHL DRSPLFSGTI EGVGPRYCPS IEDKIHRFAD
     KNSHQIFIEP EGLTTHELYP NGISTSLPFD VQLEFIRTMA GLENAHITRP GYAIEYDYFN
     PQNLKPTLET KSIDSLYFAG QINGTTGYEE AGVQGLLAGV NAALSTQDNP VMDSWTPRRD
     QAYLGVLVDD LITHGTKEPY RMFTSRAEYR LLLREDNADQ RLTEIGRKLG LVDDTRWQAY
     QQKMESMATE SARLKDLWAT PHNELGKKFT EQTGEVLSKE ATAYDLLKRP NVGFNDIAAV
     TGAQVAADVG EQIEISVKYA GYIDRQQEDI DQMKRLENTQ LPADFDYKAV SGLSNEIVQK
     LNDIRPATLA QASRISGVTP AAIQLLGMTL KKQKKAKAAL DI