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Database: UniProt
Entry: A0A4Q8QI84_9BRAD
LinkDB: A0A4Q8QI84_9BRAD
Original site: A0A4Q8QI84_9BRAD 
ID   A0A4Q8QI84_9BRAD        Unreviewed;       451 AA.
AC   A0A4Q8QI84;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase GatCAB subunit C {ECO:0000313|EMBL:TAI59976.1};
DE   Flags: Fragment;
GN   ORFNames=CWO89_43255 {ECO:0000313|EMBL:TAI59976.1};
OS   Bradyrhizobium sp. Leo170.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1571199 {ECO:0000313|EMBL:TAI59976.1, ECO:0000313|Proteomes:UP000292824};
RN   [1] {ECO:0000313|EMBL:TAI59976.1, ECO:0000313|Proteomes:UP000292824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leo170 {ECO:0000313|EMBL:TAI59976.1,
RC   ECO:0000313|Proteomes:UP000292824};
RA   Avontuur J.R., Beukes C.W., Chan W.Y., Coetzee M.P., Palmer M., Shapiro N.,
RA   Blom J., Stepkowski T., Venter S.N., Steenkamp E.T.;
RT   "Genome-informed Bradyrhizobium taxonomy: where to from here?";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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:TAI59976.1}.
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DR   EMBL; PSRR01000598; TAI59976.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Q8QI84; -.
DR   Proteomes; UP000292824; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR   PANTHER; PTHR43742:SF10; TRIMETHYLAMINE-N-OXIDE REDUCTASE 2; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000292824};
KW   Transferase {ECO:0000313|EMBL:TAI59976.1}.
FT   DOMAIN          20..205
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          322..441
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:TAI59976.1"
SQ   SEQUENCE   451 AA;  49205 MW;  F7260839F2C8D5D8 CRC64;
     IARLAAQLVG RRSYITCSFA VQRAEHGEQP YWMAIALSAL LGQVGLPGGG FGFGHGSMNG
     VGNPRPATPG PEMAVGRNPL GRAIPVARIA DMLLQPGTPY AFDGRRETYP DIKFIHWAGG
     NPFHHHQQLN RLLMGWRRPQ TIVVNEIWWT PTARLADIVL PVTTTLERND IGGSSRDRFV
     VAMHQAIAPL HEARSDFDIF ADLAARLGYE AAFTEGRDEM NWLRDIYARC AAGNAQGGIA
     FPDFENFWAE GMLELPEPNQ DFVLLGDFRA DPAAHPLKTP SGRIELYSET IAGFALPDCG
     PHPAWIEPRE WLGAESTQRF PLHLLTVQPA DRLHSQLDFA PLPQGNKVAR RECIALNPMD
     ASARGCKDGD LVRVFNDRGA CLAGVRVDAS IKSGVAVMAT GAWFDPDIEH EGAPERAGTA
     NVLTHDVGTS LLTQGPNAMS CLVEVERFTL A
//
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