ID A0A0M0HSL9_VIBNE Unreviewed; 631 AA.
AC A0A0M0HSL9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=gidA {ECO:0000256|HAMAP-Rule:MF_00129,
GN ECO:0000313|EMBL:KOO04897.1};
GN Synonyms=mnmG {ECO:0000256|HAMAP-Rule:MF_00129};
GN ORFNames=AKJ17_03145 {ECO:0000313|EMBL:KOO04897.1};
OS Vibrio nereis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=693 {ECO:0000313|EMBL:KOO04897.1, ECO:0000313|Proteomes:UP000037515};
RN [1] {ECO:0000313|Proteomes:UP000037515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19584 {ECO:0000313|Proteomes:UP000037515};
RA Giubergia S., Machado H., Mateiu R.V., Gram L.;
RT "Vibrio galatheae sp. nov., a novel member of the Vibrionaceae family
RT isolated from the Solomon Islands.";
RL Submitted (AUG-2015) 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: 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:KOO04897.1}.
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DR EMBL; LHPJ01000003; KOO04897.1; -; Genomic_DNA.
DR RefSeq; WP_053394332.1; NZ_LHPJ01000003.1.
DR AlphaFoldDB; A0A0M0HSL9; -.
DR STRING; 693.AKJ17_03145; -.
DR PATRIC; fig|693.5.peg.631; -.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000037515; 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; 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:UP000037515};
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 631 AA; 70102 MW; 5E76B5DBEDFCCB26 CRC64;
MLYHENFDVI VVGGGHAGTE AALASARTGQ KTLLLTHNID TLGQMSCNPA IGGIGKGHLV
KEVDAMGGLM AQAIDHAGIQ FRTLNASKGP AVRATRAQAD RALYKAYVRD ALENTPNLTL
FQQSVDDLIV EQDTVVGVVT QMGLKFHAKA VVLTVGTFLG GKIHIGMENF SGGRAGDPPS
IALADRLRDL PFRVDRLKTG TPPRIDARSV DFSQLEAQHG DNPTPVFSFL GERSQHPRQI
PCFITHTNEQ THDVIRSNLD RSPMYAGVIE GIGPRYCPSI EDKVMRFADK NSHQIFIEPE
GLTTHELYPN GISTSLPFDV QVQIVRSMKG FENAHIVRPG YAIEYDFFDP RDLKQTYETK
FINGLFFAGQ INGTTGYEEA AAQGLMAGLN ASLHSQGKEG WSPRRDQAYM GVLIDDLSTM
GTKEPYRMFT SRAEYRLLLR EDNADLRLTE QARELGLIDD ARWARFNEKV DNIEKERQRL
KDVWMNPKSE GIDDLNALLK TPMIREASGE DLLRRPEMTY EQLTQLEAFS PALEDQQAAE
QVEIQVKYEG YIKRQQDEIE KSLRHEHTKL PVDLDYSAVK GLSNEVIAKL NEAKPESIGI
ASRISGITPA AISILLVHLK KHGMLKKGED A
//
