ID   E6PV63_9ZZZZ            Unreviewed;       642 AA.
AC   E6PV63;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme gidA (Glucose-inhibited division protein A) {ECO:0000313|EMBL:CBH98820.1};
GN   Name=gidA {ECO:0000313|EMBL:CBH98820.1};
GN   ORFNames=CARN2_0030 {ECO:0000313|EMBL:CBH98820.1};
OS   mine drainage metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=410659 {ECO:0000313|EMBL:CBH98820.1};
RN   [1] {ECO:0000313|EMBL:CBH98820.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Bertin P.N., Heinrich-Salmeron A., Pelletier E., Goulhen-Chollet F.,
RA   Arsene-Ploetze F., Gallien S., Calteau A., Vallenet D., Casiot C.,
RA   Chane-Woon-Ming B., Giloteaux L., Barakat M., Bonnefoy V., Bruneel O.,
RA   Chandler M., Cleiss J., Duran R., Elbaz-Poulichet F., Fonknechten N.,
RA   Lauga B., Mornico D., Ortet P., Schaeffer C., Siguier P.,
RA   Alexander Thil Smith A., Van Dorsselaer A., Weissenbach J., Medigue C.,
RA   Le Paslier D.;
RT   "Diversity of trophic interactions inside an arsenic-rich microbial
RT   ecosystem.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:CBH98820.1}.
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DR   EMBL; CABM01000062; CBH98820.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6PV63; -.
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   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   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT   DOMAIN          554..625
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme C-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01228"
SQ   SEQUENCE   642 AA;  70597 MW;  0C7B98E9D9CD5545 CRC64;
     MDYPKNFDVI VVGGGHAGTE AALAAARVGA ATLLLTHNIE TLGQMSCNPS IGGIGKGHLV
     KEIDALGGAM AAATDEAGIQ FRVLNGSKGP AVRATRAQAD RLLYKADIRK RLENQTQLWL
     FQQAVDDLMI ESTGQGDRVN GAVTQSGIRF RARSVVLTAG TFLDGKIHIG LDHYAAGRAG
     DPPAISLAQR LRELKLPQGR LKTGTPPRID GRSIDFSKME EQPGDLHPIP VFSFLGRAEQ
     HPTQVPCWIT HTNSRTHDII RGGLDRSPMY TGVIEGVGPR YCPSIEDKIH RFASKDAHQI
     FLEPEGLSTH EFYPNGISTS LPFDVQLELV HSIPGLEQAH LLRPGYAIEY DYFDPRALKT
     SLETRAIGGL FFAGQINGTT GYEEAAAQGL LAGTNAALQA QGREPWCPAR DQAYLGVLVD
     DLITKGVSEP YRMFTSRAEY RLSLREDNAD LRLTEAGRKL GLVDDARWDA FCRKRDAIER
     ERQRLRSTWV QPETLSPAEA LQLVGQTIER EYRLEDLLRR PEVEYNRLVN ALEGRFAPPE
     ALQPEEAEQV QIGVKYAGYI DRQQQDVLRA AEYEHLSLPA DLDYDAVSGL SIEVRQKLGR
     ARPQTLGLAS RLSGVTPAAI SLLLVHLRKR RLRPAAAPSQ AA
//