ID A0A1I6IYI6_9BURK Unreviewed; 668 AA.
AC A0A1I6IYI6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Anaerobic selenocysteine-containing dehydrogenase {ECO:0000313|EMBL:SFR71777.1};
GN ORFNames=SAMN05428960_0452 {ECO:0000313|EMBL:SFR71777.1};
OS Mitsuaria sp. PDC51.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=1881035 {ECO:0000313|EMBL:SFR71777.1, ECO:0000313|Proteomes:UP000199246};
RN [1] {ECO:0000313|EMBL:SFR71777.1, ECO:0000313|Proteomes:UP000199246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PDC51 {ECO:0000313|EMBL:SFR71777.1,
RC ECO:0000313|Proteomes:UP000199246};
RA de Groot N.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; FOZE01000001; SFR71777.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6IYI6; -.
DR STRING; 1881035.SAMN05428960_0452; -.
DR Proteomes; UP000199246; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
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; cd02766; MopB_3; 1.
DR CDD; cd02786; MopB_CT_3; 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 Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR037920; YoaE_C.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000199246}.
FT DOMAIN 1..56
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 668 AA; 72845 MW; 4F9AE43904442FAE CRC64;
MVKGACPHDC PDTCALRITV EDGKVVKVQG QPDHPSTHGA LCTKVSRYPE RTYHAERVLH
PLKRVNAKHE PPRFERIGWD QAIAEIAGRL KAIAARDPQA ILPYSYAGTM GLLQGEAMAG
RFFNRLGASC LDRTICASAG GAALAATYGH KVGMHLPHFA ESKLILIWGS NSIASNLHFW
TFANQAKREG AKLVCIDPRK TETADKCHQH LALLPGTDGA LALGLMHELI AQDWLDHDYI
ARHVDGWDEL RAKALAWPPE RTAAECGLSA DEVRGLARDY ATLAPAAIRL NYGMQRVRGG
GNAVRLIALL PCLTGAWRHR AGGLLLSSSG WFAPFKNPAL ERPELRAGRP SRTINMSTIG
DDLLREASPD FGPRIEALVV YNSNPVAVAP ESPKVVAGFQ RPDLFTVVLE HFLTDTADLA
DYVLPATTQL EHLDIHTSYG HTDVLVNEPA VAPLGESRSN TRIFRELAAA MGFDEPAFHD
DDEALLRQAF RDDIDLAQLR ERGWFKLPLK EAPFAEGGFP SASGKADARG ADYVANYESR
SSAPALAARY PLAMISPPAR NHLNSTFVNV KSLRDIEGEQ VLEMSAGDAA ARGLADGQLV
RVFNDRGSYA CRLDVSARAR EGVVHGLGIW WRKLGADGRN VNEVTHQRLT DMGRAPCFYD
CLVEVAAA
//
