ID A0A1G5G7I0_9GAMM Unreviewed; 699 AA.
AC A0A1G5G7I0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Anaerobic selenocysteine-containing dehydrogenase {ECO:0000313|EMBL:SCY47566.1};
GN ORFNames=SAMN05661077_2223 {ECO:0000313|EMBL:SCY47566.1};
OS Thiohalorhabdus denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiohalorhabdales;
OC Thiohalorhabdaceae; Thiohalorhabdus.
OX NCBI_TaxID=381306 {ECO:0000313|EMBL:SCY47566.1, ECO:0000313|Proteomes:UP000183104};
RN [1] {ECO:0000313|Proteomes:UP000183104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL 19 {ECO:0000313|Proteomes:UP000183104};
RA Varghese N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FMUN01000006; SCY47566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5G7I0; -.
DR STRING; 381306.AN478_05775; -.
DR Proteomes; UP000183104; Unassembled WGS sequence.
DR GO; GO:0018818; F:acetylene hydratase activity; IEA:InterPro.
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 CDD; cd02781; MopB_CT_Acetylene-hydratase; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037949; MopB_CT_Acetylene-hydratase.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 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:UP000183104}.
FT DOMAIN 60..477
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 590..689
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 699 AA; 76857 MW; 75CD31A8BE181EBC CRC64;
MERESMAAEG TTWKRTTCYE CDANCAFDVA VDGAGRAVDL SGPDCPRGAA QLERQYHPER
LLQPLRRVGP RGSDRFEPIS WDEALDTIAA RLAEIRERHG AEQAAFFAGY TKEARPQLQR
LAHAFGSPNY LTESGCCFSA TLAAEKLTLG YRLKSASLLE AEQTRCLLVW STNPPASVVP
FEEHHAAQRR EGRAMVVVDP RRTRTAEAAD IHLQIRPGTD GALALAFHHV IFENGWADEA
FLKRWALGWN SLRDYAREFP PERVARICGV DAGAIRRAAE LYATSGPAQI ALSPTATVQH
SNGFQNHRAI ILLAATTGNL DIPGGNRFFL DKVRPKPIDL FRETIDDLPP RLGEETYPIW
TRYWPAGQSM LLPDAILTGE PQPIRGLFAI GINASMWPNS GRMLAALEAL EFFACSDFFL
TETAKRADIV LPAATNLERE ALVAYPGCQF RGEVRYRHSV LEPRGEARPD AQVALDLGVR
LGMAERFWHG DLAASWAEAA EGLAPEVRRQ AYEDPDGAMV FADALDEEAF EGERLYEVRG
FPTASGKVEF DSQELRAAGY DGLPVYREPA ESPASTPELA REHPFVLTSG GRSKYFTHSQ
QQRFPSLAAR DPVPRAQLHP WDAEPLEIAD GAPVEVHTPR GAVTFTAEVT DAVKPGVVHC
FHGWAGADVN RLTDHAHPDP ISGFPPFKSG LCNVAPAGE
//