ID S5R1A4_9PROT Unreviewed; 637 AA.
AC S5R1A4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG {ECO:0000256|ARBA:ARBA00020461, ECO:0000256|HAMAP-Rule:MF_00129};
DE AltName: Full=Glucose-inhibited division protein A {ECO:0000256|ARBA:ARBA00031800, ECO:0000256|HAMAP-Rule:MF_00129};
GN Name=mnmG {ECO:0000256|HAMAP-Rule:MF_00129};
GN Synonyms=gidA {ECO:0000256|HAMAP-Rule:MF_00129};
GN ORFNames=SSDC_01535 {ECO:0000313|EMBL:AGS06992.1};
OS Candidatus Profftella armatura.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Profftella.
OX NCBI_TaxID=669502 {ECO:0000313|EMBL:AGS06992.1, ECO:0000313|Proteomes:UP000015216};
RN [1] {ECO:0000313|EMBL:AGS06992.1, ECO:0000313|Proteomes:UP000015216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DC {ECO:0000313|EMBL:AGS06992.1,
RC ECO:0000313|Proteomes:UP000015216};
RX PubMed=23850282; DOI=10.1016/j.cub.2013.06.027;
RA Nakabachi A., Ueoka R., Oshima K., Teta R., Mangoni A., Gurgui M.,
RA Oldham N.J., van Echten-Deckert G., Okamura K., Yamamoto K., Inoue H.,
RA Ohkuma M., Hongoh Y., Miyagishima S.Y., Hattori M., Piel J., Fukatsu T.;
RT "Defensive bacteriome symbiont with a drastically reduced genome.";
RL Curr. Biol. 23:1478-1484(2013).
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.
CC {ECO:0000256|ARBA:ARBA00003717, ECO:0000256|HAMAP-Rule:MF_00129}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|HAMAP-Rule:MF_00129};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC {ECO:0000256|ARBA:ARBA00025948, ECO:0000256|HAMAP-Rule:MF_00129}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00129}.
CC -!- SIMILARITY: Belongs to the MnmG family. {ECO:0000256|ARBA:ARBA00007653,
CC ECO:0000256|HAMAP-Rule:MF_00129}.
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DR EMBL; CP003468; AGS06992.1; -; Genomic_DNA.
DR RefSeq; WP_020915567.1; NZ_CP041281.1.
DR AlphaFoldDB; S5R1A4; -.
DR STRING; 669502.SSDC_01535; -.
DR KEGG; ssdc:SSDC_01535; -.
DR PATRIC; fig|669502.6.peg.296; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_4; -.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000015216; 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; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.150.570; GidA associated domain, C-terminal subdomain; 1.
DR Gene3D; 1.10.10.1800; tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG/GidA; 1.
DR HAMAP; MF_00129; MnmG_GidA; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR049312; GIDA_C_N.
DR InterPro; IPR004416; MnmG.
DR InterPro; IPR002218; MnmG-rel.
DR InterPro; IPR020595; MnmG-rel_CS.
DR InterPro; IPR026904; MnmG_C.
DR InterPro; IPR047001; MnmG_C_subdom.
DR InterPro; IPR044920; MnmG_C_subdom_sf.
DR InterPro; IPR040131; MnmG_N.
DR NCBIfam; TIGR00136; gidA; 1.
DR PANTHER; PTHR11806; GLUCOSE INHIBITED DIVISION PROTEIN A; 1.
DR PANTHER; PTHR11806:SF0; PROTEIN MTO1 HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF01134; GIDA; 1.
DR Pfam; PF13932; GIDA_C; 1.
DR Pfam; PF21680; GIDA_C_1st; 1.
DR SMART; SM01228; GIDA_assoc_3; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS01280; GIDA_1; 1.
DR PROSITE; PS01281; GIDA_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00129};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_00129};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_00129};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00129};
KW Reference proteome {ECO:0000313|Proteomes:UP000015216};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00129}.
FT DOMAIN 553..624
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT BINDING 13..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 180
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 274..288
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 371
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 637 AA; 72015 MW; 78BB35B3D1F3B59A CRC64;
MLFKSKFDVI VVGGGHAGTE AALVSARMGQ KTLLLSHNID TIGQMSCNPS IGGIGKSHLV
KEIDAMGGIM AIATDKSGIQ FRILNSSKGA AVRATRAQVD RILYKQAIRF YLENQLNLYL
FQEEVDDLII KTNKILGVVT KIGIKFFSKT VILTTGTFLN GKIHIGLKSY SAGRFGDFST
TSLAKRLKEL QLSHGRLKTG TPPRIDKRTI DFSKMEEQIG DFDPVPVFSV LGNINLHPKQ
LSCFITHTNE KTHNIIRSEF KNSPIFSGKI ESIGPRYCPS IEDKVYRFPK KKSHHIFLEP
EGIVINEYYP NGISTSLPFE AQIELVQSID GMKNANIIRP GYAIEYDYFN PCNLKSSLET
KQIHGLFFAG QINGTTGYEE AASQGLLAGL NAALFSQDRD PWIPGRDQAY LGVLVDDLIT
KGIQEPYRMF TSRAEYRLNL REDNADLRLT EIGWKLGCVS YKQWKIFEKK REIITKELQR
LKDTWINPSI LNTGESERVL GKRIKHEYSL SNLLTWPNVN YNTLTSLKGI NGKNLYNTEI
YQEDIKKQLK IQLQYEGYIL RQINEVEKNK INENLKLPHN LDYMKIQSLS IEARQKLNKY
KPETIGQASR ISGVTPAALT LLLIYLKSGF LKNFIKK
//
