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Database: UniProt
Entry: H7GIT0_9DEIN
LinkDB: H7GIT0_9DEIN
Original site: H7GIT0_9DEIN 
ID   H7GIT0_9DEIN            Unreviewed;       541 AA.
AC   H7GIT0;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 2.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG {ECO:0000256|ARBA:ARBA00020461};
DE   AltName: Full=Glucose-inhibited division protein A {ECO:0000256|ARBA:ARBA00031800};
GN   ORFNames=RLTM_11238 {ECO:0000313|EMBL:EIA38435.1};
OS   Thermus parvatiensis.
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=456163 {ECO:0000313|EMBL:EIA38435.1, ECO:0000313|Proteomes:UP000053186};
RN   [1] {ECO:0000313|EMBL:EIA38435.1, ECO:0000313|Proteomes:UP000053186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RL {ECO:0000313|EMBL:EIA38435.1,
RC   ECO:0000313|Proteomes:UP000053186};
RX   PubMed=22689228; DOI=10.1128/JB.00604-12;
RA   Dwivedi V., Sangwan N., Nigam A., Garg N., Niharika N., Khurana P.,
RA   Khurana J.P., Lal R.;
RT   "Draft genome sequence of Thermus sp. strain RL, isolated from a hot water
RT   spring located atop the Himalayan ranges at Manikaran, India.";
RL   J. Bacteriol. 194:3534-3534(2012).
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}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC       {ECO:0000256|ARBA:ARBA00025948}.
CC   -!- SIMILARITY: Belongs to the MnmG family.
CC       {ECO:0000256|ARBA:ARBA00007653}.
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:EIA38435.1}.
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DR   EMBL; AIJQ01000017; EIA38435.1; -; Genomic_DNA.
DR   PATRIC; fig|456163.3.peg.2098; -.
DR   Proteomes; UP000053186; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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   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.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          464..535
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme C-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01228"
FT   UNSURE          419
FT                   /note="E or Q"
FT                   /evidence="ECO:0000313|EMBL:EIA38435.1"
SQ   SEQUENCE   541 AA;  59849 MW;  AA8EF7A8CDB5B045 CRC64;
     MAEVVALGGL MGRAADAAAI HTRVLNRSKG PAVQSLRVQV DRDLYALKAQ EILAERPVEV
     LRGEVAALWV EGGRLLGVRT VDGRTLPAKA VVVAGGTFLS GVVWYGRKSR PAGRQGEPPA
     RFLSQSLKAV GHTLRRFKTG TPPRIRADSV DFGRLEVVPP EVPPGSFTGN PGPXAXRLPT
     WQTRTTXXTH RLIXENLHLS PLYAGDIQGI GPRYCPSIED KVVRFADKES HLLFVEPDGL
     STTEVYLQGF SSSLPPELQE XMVRXLPGFE RAVIQRYAYA VEYDSLDPTE LTRGLQSRXL
     PGLFSAGQVN GTSGYEEAAA QGXLAGLNAA RFALGLPEVH LPRESGYIGV LVDDLVGRGT
     DEPYRMMTSR VELRLLCRAD NADERLTPLA VAWGLRPRED LERVEAKYRR VAXELRRLEA
     LRVEGVSGLQ WLRRPENTYR ALXERFPPPE PLSPEEAYQV EVRAKYAGYI ERQERLREKM
     XDLEAFRIPE GMDFPKVPGL SREAAEKLSR HRPKSLAEAA RIPGVRDSDL TALAVHLRRG
     A
//
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