ID A0A420EEH8_9SPHN Unreviewed; 620 AA.
AC A0A420EEH8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
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 ECO:0000313|EMBL:RKF19056.1};
GN Synonyms=gidA {ECO:0000256|HAMAP-Rule:MF_00129};
GN ORFNames=D6851_13635 {ECO:0000313|EMBL:RKF19056.1};
OS Altericroceibacterium spongiae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Altericroceibacterium.
OX NCBI_TaxID=2320269 {ECO:0000313|EMBL:RKF19056.1, ECO:0000313|Proteomes:UP000284395};
RN [1] {ECO:0000313|EMBL:RKF19056.1, ECO:0000313|Proteomes:UP000284395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HN-Y73 {ECO:0000313|EMBL:RKF19056.1,
RC ECO:0000313|Proteomes:UP000284395};
RA Zhuang L., Luo L.;
RT "Altererythrobacter spongiae sp. nov., isolated from a marine sponge.";
RL Submitted (SEP-2018) 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.
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}.
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:RKF19056.1}.
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DR EMBL; RAPF01000007; RKF19056.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420EEH8; -.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000284395; 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 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.
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:UP000284395};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00129}.
FT DOMAIN 537..608
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT BINDING 10..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 269..283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 620 AA; 67565 MW; 24641FB3443857BD CRC64;
MHEFDILVVG GGHAGCEAAS VAARMGARAG LINFDLTTLG AMSCNPAIGG LGKGHLVREV
DAFDGLIGRA ADFAAIHYRM LNRSKGSAVW GPRVQADREL FREAVQRMLK QQGNLALIEG
EVAELVFEGE RVAGLKLGDG QKLVAQAVIL CTGTFLGGTL FRGEERFTGG RIGENSAQRL
AEQLRETNLP MARLKTGTPP RLDGHTINWA VLDEQPSDSD FWTMSPMSQE RVNPQLFCAI
SRTNPRSHDI IRANLDRSPL FSGAIGAAGP RYCPSIEDKI HRFADRDGHQ IFLEPEGLRT
HLVYPNGIST SLPVDVQLAM LRSMKGLEQV DMVVPGYAVE YDHIDPRSLS AGLEVRQIPG
LYCAGQINGT TGYEEAAAQG LVAGMHAAAR ALGRDPAALD RSNSYMAVMI DDLTLHGVSE
PYRMLTSRAE YRLRLRANNA TTRLSPLADA TGCLSPARQK WFAERRKAQS RWNEALDRKV
HSIDLADAGL PVRRDSGALP LREWLRFGGV TLESLADWLP EECDSNSDVG QEAAEDSIYA
PYLARQNAEL RDLKASDQLT LPHDFPYDRV PGLSNEMIER LQAAQPETLA VAGRVRGITP
AALAALLVHA KRIQNVTDAA
//
