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Database: UniProt
Entry: T2SLB7_HELPX
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Original site: T2SLB7_HELPX 
ID   T2SLB7_HELPX            Unreviewed;       621 AA.
AC   T2SLB7;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=L932_02750 {ECO:0000313|EMBL:EQD93516.1};
OS   Helicobacter pylori PZ5026.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1337392 {ECO:0000313|EMBL:EQD93516.1, ECO:0000313|Proteomes:UP000015722};
RN   [1] {ECO:0000313|EMBL:EQD93516.1, ECO:0000313|Proteomes:UP000015722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PZ5026 {ECO:0000313|EMBL:EQD93516.1,
RC   ECO:0000313|Proteomes:UP000015722};
RX   PubMed=24051318;
RA   Sheh A., Piazuelo M.B., Wilson K.T., Correa P., Fox J.G.;
RT   "Draft Genome Sequences of Helicobacter pylori Strains Isolated from
RT   Regions of Low and High Gastric Cancer Risk in Colombia.";
RL   Genome Announc. 1:e00736-13(2013).
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:EQD93516.1}.
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DR   EMBL; ASYT01000079; EQD93516.1; -; Genomic_DNA.
DR   RefSeq; WP_021173148.1; NZ_ASYT01000079.1.
DR   AlphaFoldDB; T2SLB7; -.
DR   PATRIC; fig|1337392.3.peg.517; -.
DR   Proteomes; UP000015722; 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   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00129}.
FT   DOMAIN          542..613
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         270..284
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   621 AA;  69733 MW;  2269F40D7F7FB40D CRC64;
     MVKESDILVV GGGHAGIEAS LIAAKMGARV HLITMLIDTI GLASCNPAIG GLGKGHLTKE
     VDVLGGAMGI ITDHSGLQYR VLNASKGPAV RGTRAQIDMD TYRIFARNLV LNTPNLSVSQ
     EMTESLILEN DEVVGVTTNI NNTYRAKKVI ITTGTFLKGV VHIGEHQNQN GRFGENASNS
     LALNLRELGF KVERLKTGTC PRVAGNSIDF EGLEEHFGDT NPPYFSYKTK DFNPTQLSCF
     ITYTNPITHQ IIRDNFHRAP LFSGQIEGIG PRYCPSIEDK INRFSEKERH QLFLEPQTIH
     KSEYYINGLS TSLPLDVQEK VIHSIKGLEN ALITRYGYAI EYDFIQPTEL THTLETKKIK
     GLYLAGQING TTGYEEAAAQ GLMAGINAVL ALKNQAPFIL KRNEAYIGVL IDDLVTKGTN
     EPYRMFTSRA EYRLLLREDN TLFRLGEHAY NLGLMEEYFY KELKKDQQAI QENLKRLREC
     VLTPSKEVLK RLNELDENPI NDKVDGVSLL ARDSFNIEKM RSFFSFLAPL NERVLEQIKI
     ECKYNIYIEK QHENIAKMDS MLKVSIPKDF VFKGIPGLSL EAVEKLEKFR PKSLFEASEI
     SGITPANLDV LHLYIHLRKN S
//
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