ID   MNMG_DINSH              Reviewed;         619 AA.
AC   A8LPC3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   01-MAY-2013, entry version 41.
DE   RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG;
DE   AltName: Full=Glucose-inhibited division protein A;
GN   Name=mnmG; Synonyms=gidA; OrderedLocusNames=Dshi_3455;
OS   Dinoroseobacter shibae (strain DFL 12).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Dinoroseobacter.
OX   NCBI_TaxID=398580;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DFL 12;
RX   PubMed=19741735; DOI=10.1038/ismej.2009.94;
RA   Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I.,
RA   Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S.,
RA   Han C., Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N.,
RA   Liebl W., Liesegang H., Meincke L., Pati A., Petersen J.,
RA   Piekarski T., Pommerenke C., Pradella S., Pukall R., Rabus R.,
RA   Stackebrandt E., Thole S., Thompson L., Tielen P., Tomasch J.,
RA   von Jan M., Wanphrut N., Wichels A., Zech H., Simon M.;
RT   "The complete genome sequence of the algal symbiont Dinoroseobacter
RT   shibae: a hitchhiker's guide to life in the sea.";
RL   ISME J. 4:61-77(2010).
CC   -!- FUNCTION: NAD-binding protein involved in the addition of a
CC       carboxymethylaminomethyl (cmnm) group at the wobble position (U34)
CC       of certain tRNAs, forming tRNA-cmnm(5)s(2)U34 (By similarity).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity). Heterotetramer of two MnmE and
CC       two MnmG subunits (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the MnmG family.
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DR   EMBL; CP000830; ABV95188.1; -; Genomic_DNA.
DR   RefSeq; YP_001534789.1; NC_009952.1.
DR   ProteinModelPortal; A8LPC3; -.
DR   STRING; 398580.Dshi_3455; -.
DR   EnsemblBacteria; ABV95188; ABV95188; Dshi_3455.
DR   GeneID; 5712513; -.
DR   KEGG; dsh:Dshi_3455; -.
DR   PATRIC; 21819721; VBIDinShi9476_3589.
DR   eggNOG; COG0445; -.
DR   HOGENOM; HOG000201059; -.
DR   KO; K03495; -.
DR   OMA; AQMSCNP; -.
DR   ProtClustDB; PRK05192; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:HAMAP.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR   HAMAP; MF_00129; MnmG_GidA; 1; -.
DR   InterPro; IPR004416; GidA.
DR   InterPro; IPR026904; GidA-assoc_3.
DR   InterPro; IPR002218; GIDA-rel.
DR   InterPro; IPR020595; GIDA-rel_CS.
DR   Pfam; PF01134; GIDA; 1.
DR   Pfam; PF13932; GIDA_assoc_3; 1.
DR   TIGRFAMs; TIGR00136; gidA; 1.
DR   PROSITE; PS01280; GIDA_1; 1.
DR   PROSITE; PS01281; GIDA_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; NAD; tRNA processing.
FT   CHAIN         1    619       tRNA uridine 5-carboxymethylaminomethyl
FT                                modification enzyme MnmG.
FT                                /FTId=PRO_1000076316.
FT   NP_BIND      12     17       FAD (By similarity).
FT   NP_BIND     271    285       NAD (Potential).
FT   BINDING     124    124       FAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     179    179       FAD (By similarity).
FT   BINDING     368    368       FAD (By similarity).
SQ   SEQUENCE   619 AA;  67314 MW;  D14D485A6AD3E96A CRC64;
     MKQQAFDVIV IGGGHAGTEA AAAAARLGVQ VALITLERSG IGVMSCNPAI GGLGKGHLVR
     EIDAMDGVMG RVADKAGIQF RLLNRRKGPA VQGPRSQSDR DVYRSEMLAE MESLPNLRIL
     EGEVADLITS GTRIEGVCLA DGSEVTARAV VVTTGTFLRG IIHIGNRSFQ GGRMGAAPSV
     RLAERFDSFG LPLGRLKTGT PPRLDKRSIA WDKLEPQPGD EDPTLFSFLS AGPHLRQVHC
     AVTHTNERTH EIIRKNLSRS AMYGGSIEGV GPRYCPSIED KVVRFSDKTS HQIFLEPEGL
     DSTTIYPNGI STSLPEDVQE AYVRSISGLE NAKITQPGYA IEYDYVDPRA LDAALRVKGF
     DGLYLAGQIN GTTGYEEAAA QGLVAGLNAA LEGKGKFLPS RMTSYIGVMI DDLITQGVAE
     PYRMFTSRAE YRLSLRCDNA DQRLTPEGLV LGCVGKERRI KFEKKMGLLD ETLKKLKSFE
     VTPKQANEAG IRVNEDGRRR SGLDLLSLSN VSYESLAATW PELQASTEIA KQAKIEATYA
     NYIERQQRDV MALKKDEEIE FPPRFDFSGL SGLSNELKSK LTAVRPSTLG QAARIEGMTP
     AALTLLLASL RKAEKRRSA
//