ID E9CMM6_9GAMM Unreviewed; 629 AA.
AC E9CMM6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
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=SSYM_1592 {ECO:0000313|EMBL:EFW12182.1};
OS Serratia symbiotica str. Tucson.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia; Serratia symbiotica.
OX NCBI_TaxID=914128 {ECO:0000313|EMBL:EFW12182.1, ECO:0000313|Proteomes:UP000013568};
RN [1] {ECO:0000313|Proteomes:UP000013568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson {ECO:0000313|Proteomes:UP000013568};
RX PubMed=21266540;
RA Burke G.R., Moran N.A.;
RT "Massive genomic decay in Serratia symbiotica, a recently evolved symbiont
RT of aphids.";
RL Genome Biol. Evol. 3:195-208(2011).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00129}.
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DR EMBL; GL636115; EFW12182.1; -; Genomic_DNA.
DR RefSeq; WP_006708945.1; NZ_GL636115.1.
DR AlphaFoldDB; E9CMM6; -.
DR HOGENOM; CLU_007831_2_2_6; -.
DR Proteomes; UP000013568; Unassembled WGS sequence.
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; IPR000048; IQ_motif_EF-hand-BS.
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.
DR PROSITE; PS50096; IQ; 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:UP000013568};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00129}.
FT DOMAIN 546..617
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 273..287
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 629 AA; 70303 MW; 0A8787AFA4F9E670 CRC64;
MFYPDQFDVI IIGGGHAGTE AAMAAARMGR QTLLLTHNID TLGQMSCNPA IGGIGKGHLV
KEIDALGGLM ATAIDHAGIQ FRILNASKGP AVRATRAQAD RVLYRQAIRT ALENKPNLMI
FQQPVDDLIV ENDHAVGAVT QMGLKFRAKA VVLTVGTFLD GKIHIGLKNY RGGRAGDPTA
ISLSQRLREL PLRVNRLKTG TPPRIDARTI NFSVLMPQQG DTPVPVFSFM GNASQHPEQR
TCYITHTNEK THEVIRNNLD RSPMYSGIIE GIGPRYCPSI EDKVMRFADR NTHQIFLEPE
GLTSNEIYPN GISTSLPFDV QMQIVRSMEG MQNARIVRPG YAIEYDFFDP RDLKPTLESK
FIQGLFFAGQ INGTTGYEEA AAQGLLAGLN AGRYANQDEG WAPRRDQSYL GVLVDDLSTL
GTKEPYRMFT SRAEYRLMLR EDNADLRLTE KGRDLGLVDD VRWARYCEKL EHIEQERQRL
RDIWMHPHAE NVEQVNLLLK TPLSREANGE ELLRRPEMDY SLLTSVAAFS PALEDTQAAE
QVEIQVKYQG YIARQQEEIE KQQRNENTVL PLDLDYCQVS GLSNEVIAKL NDHKPNSIGQ
ASRISGITPA AISILLIWLK KQGLLRRSA
//
