ID A0A329N755_9FLAO Unreviewed; 623 AA.
AC A0A329N755;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=DN748_07590 {ECO:0000313|EMBL:RAV29362.1};
OS Sinomicrobium sp. N-1-3-6.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Sinomicrobium.
OX NCBI_TaxID=2219864 {ECO:0000313|EMBL:RAV29362.1, ECO:0000313|Proteomes:UP000250485};
RN [1] {ECO:0000313|EMBL:RAV29362.1, ECO:0000313|Proteomes:UP000250485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N-1-3-6 {ECO:0000313|EMBL:RAV29362.1,
RC ECO:0000313|Proteomes:UP000250485};
RA Liu X., Lai Q., Shao Z.;
RT "Sinomicrobium soli sp. nov., isolated from arctic soil.";
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:RAV29362.1}.
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DR EMBL; QLNV01000005; RAV29362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A329N755; -.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000250485; 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:UP000250485};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00129}.
FT DOMAIN 548..619
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT BINDING 12..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 272..286
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 623 AA; 70059 MW; CE4398088CA35B9D CRC64;
MFDSTYDVIV VGAGHAGSEA AAAAANMGSR TLLITMNLQN IAQMSCNPAM GGIAKGQIVR
EIDAMGGYSG IVTDRTAIQF KMLNKSKGPA MWSPRAQSDR MRFAEEWRLM LEQTPNLDFY
QEMVSGLLVE NGKITGVKTS LGIEIKAKAV VLTNGTFLNG LIHIGEKQFG GGRAGERAAT
GITEDLINLG FDAGRMKTGT PPRVDGRSLD YSVMQEQPGD DIPEKFSYSD LTRPLEKQRS
CHMTYTSPEV HDLLREGFDR SPMFNGRIKS IGPRYCPSIE DKINRFADKD RHQLFVEPEG
WNTVEVYVNG FSTSLPEEVQ FKALRSVTGF ENVKFFRPGY AIEYDYFPPT QLRHTLETKL
VENLFFAGQI NGTTGYEEAA SQGLIAGMNA HLKVFGKDPF ILKRSEAYIG VLIDDLITKG
TEEPYRMFTS RAEYRTLLRQ DNADFRLTPR SHAVGLASGE RLRRMEKKKD NADAFIHFFR
ETSVDPSEMN PVLEEKKSSL MKQSDKMYKV FSRPNITMDD MMKIGEVRQY AEHHQLDKEV
LEQTEIQVKY SGYIEKEKNN ADKLNRLEDI AIPSGFDYDK LKSLSFEARE KLKHIRPATL
SQASRISGVS PSDISVMLVY MGR
//
