ID A0A2G8ECL0_9GAMM Unreviewed; 629 AA.
AC A0A2G8ECL0;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=BK416_09635 {ECO:0000313|EMBL:PIJ72282.1};
OS Erwinia sp. OLSSP12.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=1912096 {ECO:0000313|EMBL:PIJ72282.1, ECO:0000313|Proteomes:UP000229786};
RN [1] {ECO:0000313|EMBL:PIJ72282.1, ECO:0000313|Proteomes:UP000229786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLSSP12 {ECO:0000313|EMBL:PIJ72282.1,
RC ECO:0000313|Proteomes:UP000229786};
RX PubMed=29067021; DOI=10.3389/fmicb.2017.01969;
RA Chen X., Hitchings M.D., Mendoza J.E., Balanza V., Facey P.D., Dyson P.J.,
RA Bielza P., Del Sol R.;
RT "Comparative Genomics of Facultative Bacterial Symbionts Isolated from
RT European Orius Species Reveals an Ancestral Symbiotic Association.";
RL Front. Microbiol. 8:1969-1969(2017).
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIJ72282.1}.
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DR EMBL; MNCH01000024; PIJ72282.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8ECL0; -.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000229786; 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:UP000229786};
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 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 273..287
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 370
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 629 AA; 69868 MW; 9797EA9724ECA616 CRC64;
MFYPDPFDVI VIGGGHAGTE AAMAAARTGQ QTLLLTHNID TLGQMSCNPA IGGIGKGHLV
KEVDALGGLM ATATDKAGIQ FRILNASKGP AVRATRAQAD RVLYRQAVRS ALENQPNLMI
FQQAVDDLIV ENHRVVGVVT QMGLKFKAKA VVLTVGTFLD GKIHIGMDNY SGGRAGDPPS
IPLARRLREL PLRVSRLKTG TPPRIDARSI DFTQLATQHG DNPMPVFSFM GSADQHPQQM
PCWMTYTNEQ THDTIRKNLD RSPMFAGIIE GIGPRYCPSI EDKVVRFADR TAHQIFLEPE
GLTSNEIYPN GISTSLPFDV QMQIVRSIKG MENARIVRPG YAIEYDFFDP RDLKSTLENK
FIHGLFFAGQ INGTTGYEEA AAQGLLAGLN AARFSAEKEG WAPRRDQAYL GVLVDDLCTL
GTKEPYRMFT SRAEYRLLLR EDNADLRLTA IGRELGLVDD IRWARYNQKL EQIERERQRL
RDTWLHPKSS NVAEINALLS APLTKEANGE DLLRRPEMTY QQLMTLSTFG DALADDQAAE
QVEIQVKYEG YIARQQEEIL RQMRNENTLL PVDLDYLQVS GLSNEVRAKL NDHKPGSIGQ
ASRISGITPA AISILLIWLK KQGLLRKSA
//
