ID X7EAB9_9GAMM Unreviewed; 629 AA.
AC X7EAB9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=MUS1_00700 {ECO:0000313|EMBL:ETX12161.1};
OS Marinomonas ushuaiensis DSM 15871.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=1122207 {ECO:0000313|EMBL:ETX12161.1, ECO:0000313|Proteomes:UP000054058};
RN [1] {ECO:0000313|EMBL:ETX12161.1, ECO:0000313|Proteomes:UP000054058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15871 {ECO:0000313|EMBL:ETX12161.1,
RC ECO:0000313|Proteomes:UP000054058};
RA Lai Q., Shao Z.S.;
RT "Marinomonas ushuaiensis DSM 15871 Genome Sequencing.";
RL Submitted (JAN-2014) 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:ETX12161.1}.
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DR EMBL; JAMB01000001; ETX12161.1; -; Genomic_DNA.
DR RefSeq; WP_036157703.1; NZ_JAMB01000001.1.
DR AlphaFoldDB; X7EAB9; -.
DR STRING; 1122207.MUS1_00700; -.
DR PATRIC; fig|1122207.3.peg.146; -.
DR eggNOG; COG0445; Bacteria.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000054058; 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 PRINTS; PR00411; PNDRDTASEI.
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:UP000054058};
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; 69812 MW; 2FAE65D537DEC260 CRC64;
MDFPSRFDVI VVGGGHAGTE AALAAARMGV KTLLLSHNIE TLGQMSCNPA IGGIGKSHLV
KEIDALDGAM GLATDQAGIQ FRTLNSRKGP AVRATRAQAD RILYKAAIRH KLENQENLWL
FQQSAEDLIV EDGEARGVIT QTGIRFNSKT VVLTAGTFLG GVIHIGLQNH SGGRAGDPPS
IGLAEKLRAL PFRVDRLKTG TPPRIDARSV DFSQMQAQPG DDITPVMSYM GNRAMHPRQI
ECFITHTNER THDIIRSGMD RSPMYTGVIE GVGPRYCPSI EDKIVRFADK NSHQIFIEPE
GLTTHELYPN GISTSLPFDV QIELVRSMKG MENAHIIRPG YAIEYDYFNP QDLKYSLETK
HMPGLFFAGQ INGTTGYEEA GAQGLLAGLN AALLAQDKEA WTPRRDEAYL GVLVDDLITM
GTKEPYRMFT SRAEYRLILR EDNADMRLTE KGRELGLVSD ERWAAFCKKR EAIEVETERL
KSTWIVPNSP ESEVLNPKLE TPITHEYSLL ELLKRPNIVY SDIANLKNIP DESVDEQVSE
QVQIAVKYSG YITRQAEDIE RLRRQENTPL PDDLDYSNME GLSNEVKQKL TEIRPATLAA
ASRIQGITPA AVSLLLIHLK KRAIARKSA
//
