ID A0A0W0VCK5_9GAMM Unreviewed; 642 AA.
AC A0A0W0VCK5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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:KTD17816.1};
GN Synonyms=mnmG {ECO:0000256|HAMAP-Rule:MF_00129};
GN ORFNames=Ljor_2122 {ECO:0000313|EMBL:KTD17816.1};
OS Legionella jordanis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=456 {ECO:0000313|EMBL:KTD17816.1, ECO:0000313|Proteomes:UP000055035};
RN [1] {ECO:0000313|EMBL:KTD17816.1, ECO:0000313|Proteomes:UP000055035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL-540 {ECO:0000313|EMBL:KTD17816.1,
RC ECO:0000313|Proteomes:UP000055035};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-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: 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:KTD17816.1}.
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DR EMBL; LNYJ01000011; KTD17816.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0VCK5; -.
DR STRING; 456.Ljor_2122; -.
DR PATRIC; fig|456.5.peg.2278; -.
DR Proteomes; UP000055035; 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:UP000055035};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00129}.
FT DOMAIN 562..633
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT BINDING 31..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 291..305
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 642 AA; 70843 MW; 738CE4831BD30BA9 CRC64;
MLLKKCIIEG FVAQFFPHMN LETVYDVIVV GGGHAGTEAA LAAARMGAKT LLLTHNMDML
GQMSCNPAIG GIGKGHLVKE IDALDGAMAL AADEAGIQFR ILNASKGPAV RATRAQADRV
LYRQAIRHQL QNQSNLTLFQ QAVDDILIEG DRVSAVVTQI GLILKAQAIV LTVGTFLGGK
IHVGMNQYAG GRAGDPPAIA LAQRLRELAL PVGRLKTGTP PRIDGRSLDY SQMSVQPGDE
PVPVFSYLGN PSLHPKQVPC YITHTTAQTH EIIQQNLHQS PMYAGVIEGI GPRYCPSIED
KIVRFADKSS HQIFVEPEGL TTHEIYPNGI STSLPFEVQV QFVRTIKGFE QAHITRPGYA
IEYDYFDPRG LTPYLQTKAL SNLFFAGQIN GTTGYEEAAA QGLIAGMNAA LQTQDKELWS
PRRDEAYVGV LIDDLITCGT QEPYRMFTSR AEYRLLLRED NADLRLTEKG RELGLVGDKR
WQVFCEKREA IEKARAQLKD SIVRVSHNEQ LQHVLENPLQ QDCKAAELLK RPEVRYGDLQ
AVEALNLAAL PDDVAEQVEI QSKYAGYIER QLLDIERLRK HENTQLPADL DYNKVSGLSN
EVMQKLSRIR PTTLAQAGRI SGVTPAALSL LLVHLKKHRE SA
//
