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Database: UniProt
Entry: A0A3D8PCC2_9RHOB
LinkDB: A0A3D8PCC2_9RHOB
Original site: A0A3D8PCC2_9RHOB 
ID   A0A3D8PCC2_9RHOB        Unreviewed;       773 AA.
AC   A0A3D8PCC2;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase GatCAB subunit C {ECO:0000313|EMBL:RDW12911.1};
GN   ORFNames=DIE28_11065 {ECO:0000313|EMBL:RDW12911.1};
OS   Paracoccus thiocyanatus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=34006 {ECO:0000313|EMBL:RDW12911.1, ECO:0000313|Proteomes:UP000256679};
RN   [1] {ECO:0000313|EMBL:RDW12911.1, ECO:0000313|Proteomes:UP000256679}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SST {ECO:0000313|EMBL:RDW12911.1,
RC   ECO:0000313|Proteomes:UP000256679};
RA   Ghosh W., Rameez M.J., Roy C.;
RT   "Whole genome sequencing of Paracoccus thiocyanatus SST.";
RL   Submitted (MAY-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:RDW12911.1}.
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DR   EMBL; QFCQ01000060; RDW12911.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8PCC2; -.
DR   Proteomes; UP000256679; 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   CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR   CDD; cd02769; MopB_DMSOR-BSOR-TMAOR; 1.
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   Gene3D; 3.90.55.10; Dimethylsulfoxide Reductase, domain 3; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR041954; CT_DMSOR/BSOR/TMAOR.
DR   InterPro; IPR041460; Molybdopterin_N.
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; PF18364; Molybdopterin_N; 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; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000256679};
KW   Transferase {ECO:0000313|EMBL:RDW12911.1}.
FT   DOMAIN          4..42
FT                   /note="Molybdopterin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18364"
FT   DOMAIN          46..500
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          616..736
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   REGION          748..773
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   773 AA;  84158 MW;  60F9F644717FE037 CRC64;
     MIVTHWGVYH AEMRDGRPAR LVPVADDPAP SPIADGMLDA LHSPARILRP AVRRSFLTGQ
     AGAGRGAEPF VELPWDEALD LAAGHLRRIR DEHGNQAIFG GSYGWSSAGR FHHAQSQVHR
     FLNMMGGYTR SVQNYSFAAA DVILPHVTGD SRGVAKGHTL LRDIAQHTEL LIAFGGLPAK
     NAQVSAGGIL RHILPGSVAA AERNGARMVN ISPIRDDIEG RHDVDWIPIR PNTDVALMLG
     LAHVLASEGL HDRAFLDSHA TGYDRFEDYL LGRADGTPKT PEWAAAICGV PADSIRDLAR
     AMPRHRTMIA MAWSLQRADH GEQPYWMAIT LAAMLGQIGL PGGGYGFGYA SVGGIGAPAA
     AVAWPSLPQG RNPVQEFIPV ARIADMLLGP GERYDYNGQS RVYPDIRAVY WAGGNPFHHH
     QDLNRLRRAW QKPDLVIVHD SWWNPVARHA DIVFPVTTAL ERNDIACSSR DTFIAPSHKL
     AEPAGETRPD YEIFAALAKR LGCWQEFTEG RDEEAWLRHL YDLACEQAVG SGVNMPDFET
     FWQEGLRDLP EAAQQPPLFA AYRADPAANA LRTPSGRIEI HSAVIEKFGY ADCPGHPAWL
     EPLEWLGSEK TRDYPLHLLS NQPKTRLHSQ YDVGSHSRAS KIKGREPMRM HPDDAAARGI
     REGDLVRVFN GRGACLAGVT LSDALMPGVV QLSTGAWFDP DDPAAAMPLE KHGNPNVLTR
     DAGTSRLAQG PSANSCLVEV EPFRQAPPAV TAFTPPELAP AGPGSAPSLT QKT
//
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