ID A0A2W1MZJ8_9FLAO Unreviewed; 624 AA.
AC A0A2W1MZJ8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=DNU06_11895 {ECO:0000313|EMBL:PZE16690.1};
OS Putridiphycobacter roseus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Crocinitomicaceae; Putridiphycobacter.
OX NCBI_TaxID=2219161 {ECO:0000313|EMBL:PZE16690.1, ECO:0000313|Proteomes:UP000249248};
RN [1] {ECO:0000313|EMBL:PZE16690.1, ECO:0000313|Proteomes:UP000249248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM1701 {ECO:0000313|EMBL:PZE16690.1,
RC ECO:0000313|Proteomes:UP000249248};
RA Zhang X.;
RT "The draft genome sequence of Crocinitomix sp. SM1701.";
RL Submitted (JUN-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:PZE16690.1}.
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DR EMBL; QKSB01000007; PZE16690.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W1MZJ8; -.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000249248; 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:UP000249248};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00129}.
FT DOMAIN 549..620
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT BINDING 11..16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 271..285
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 624 AA; 69183 MW; F758736F70C3FBB0 CRC64;
MLQEYDVIVV GGGHAGCEAA HAAAKMGSST LLVTMNLATI AQMSCNPAMG GVAKGQIVRE
IDALGGGSGI VSDQSAIQFR MLNLSKGPAM WSPRTQNDRM LFAAKWREKL EQTEKLDFWQ
DMATGIVVEN DKVVGVKTSL GMVIKCKSIV LTNGTFLNGK IHLGEKQFKG GRAGESASYG
ITENLIDLGF ESGRMKTGTP PRVDGRSLDY SKMEEQAGDV SPFKFSYAKE SDYLQKQLPC
HITYTNPATH EMLKTGFDRS PMFNGAIKSA GPRYCPSIED KINRFAERDR HQIFVEPEGW
NTVEIYVNGF STSLPEDVQL NALRTIVGFE NVKMFRPGYA IEYDYFPPTQ LKHTLETKIV
ENLYFAGQIN GTTGYEEAAA QGLMAGINAH LKLRKKEPFI LKRSDAYIGV LIDDLITKGT
KEPYRMFTSR AEFRILLRQD NADLRLTALG HEIGLADENR YINVLKKSED TQAIKTLLEN
TSVSPTEMNE YLLSINSSPL KQKQKANVLL SRPHVKLSEM EINSPQLTKQ LSAYKATSFD
AVEQAEIQIK YDGYISREQE MANKMIRLEN VKIPLDIDYS VFSSLSAEAV EKLTAIQPVT
IGQASRISGV SPSDISVLLV FLGR
//
