ID A5TVM1_FUSNP Unreviewed; 633 AA.
AC A5TVM1;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 87.
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=gidA3 {ECO:0000313|EMBL:EDK88946.1};
GN Synonyms=gidA {ECO:0000256|HAMAP-Rule:MF_00129}, mnmG
GN {ECO:0000256|HAMAP-Rule:MF_00129};
GN ORFNames=FNP_1159 {ECO:0000313|EMBL:EDK88946.1};
OS Fusobacterium polymorphum ATCC 10953.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=393480 {ECO:0000313|EMBL:EDK88946.1};
RN [1] {ECO:0000313|EMBL:EDK88946.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10953 {ECO:0000313|EMBL:EDK88946.1};
RA Qin X., Weinstock G.M.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDK88946.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10953 {ECO:0000313|EMBL:EDK88946.1};
RA Karpathy S.E., Xiang Q., Gioia J., Jiang H., Liu Y., Petrosino J.F.,
RA Yerrapragada S., Fox G.E., Kinder Haake S., Weinstock G.M.,
RA Highlander S.K.;
RT "Genome sequence of Fusobacterium nucleatum subspecies polymorphum - a
RT genetically tractable Fusobacterium.";
RL Submitted (MAY-2007) 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}.
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DR EMBL; CM000440; EDK88946.1; -; Genomic_DNA.
DR RefSeq; WP_005897484.1; NZ_CM000440.1.
DR AlphaFoldDB; A5TVM1; -.
DR GeneID; 45634139; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_0; -.
DR Proteomes; UP000001921; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; PR00368; FADPNR.
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 Cell cycle {ECO:0000313|EMBL:EDK88946.1};
KW Cell division {ECO:0000313|EMBL:EDK88946.1};
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 tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00129}.
FT DOMAIN 555..626
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT BINDING 10..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 122
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 181
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 277..291
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 374
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 633 AA; 71243 MW; DC07AAA94B2CBC55 CRC64;
MQEFDIIVVG AGHAGCEAAL ASARMGMKTA VFTISLDNIG VMSCNPSLGG PAKSHLAREI
DALGGEMGRN IDKTFIQIRV LNTKKGPAVR SLRAQADKMT YANEMKKTLE HTDNLSVIQG
MVSELIVEEE NGKKVIKGIK IREGLEYRAK IVILATGTFL RGLIHIGEVN FSAGRMGELS
SEDLPLSLEK VGLKLGRFKT GTPARIDGRT IDFSVLEEQP GDKSQVLKFS NRTTDKEALS
RRQISCYIAH TNEKVHEIIK NSKERSPMFN GKIQGLGPRY CPSIEDKVFR YPDKNQHHLF
LEREGYETNE IYLGGMSSSL PVDVQEEMIK NLQGFENAKI MRYAYAIEYD YVPPEEIKYT
LESRTIDNLF LAGQINGTSG YEEAGAQGLM AGINAVRKLR NEEPIILDRA DSYIGTLIDD
LVSKGTNEPY RMFTARSEYR LYLREDNADL RLSKIGYELG LIPEEEYQRV EKKRRDVELI
TEILTKTSVG PSNPRVNETL LKRGENPIKD GSTLLELLRR PEVTFKDIEY ISEEIKGVDL
QGYDHDTTYQ VEITVKYQGY INRALKMIEK HKSMENKKIP ADIDYDDLKT IPKEAKDKLK
RIKPINIGQA SRISGVSPAD IQAILIYLKM RGN
//
