ID A0A1H2EY33_9FLAO Unreviewed; 704 AA.
AC A0A1H2EY33;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Anaerobic selenocysteine-containing dehydrogenase {ECO:0000313|EMBL:SDU00050.1};
GN ORFNames=SAMN04487762_1199 {ECO:0000313|EMBL:SDU00050.1};
OS Polaribacter sp. Hel1_33_78.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1336804 {ECO:0000313|EMBL:SDU00050.1, ECO:0000313|Proteomes:UP000198843};
RN [1] {ECO:0000313|EMBL:SDU00050.1, ECO:0000313|Proteomes:UP000198843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hel1_33_78 {ECO:0000313|EMBL:SDU00050.1,
RC ECO:0000313|Proteomes:UP000198843};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; LT629794; SDU00050.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2EY33; -.
DR STRING; 1336804.SAMN04487762_1199; -.
DR OrthoDB; 9792592at2; -.
DR Proteomes; UP000198843; Chromosome i.
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 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; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
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.
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:UP000198843}.
FT DOMAIN 2..59
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 704 AA; 78644 MW; 0761ECC26C353EA8 CRC64;
MSEITKYRTC HLCEAMCGVE IILKKNKIKK ISGDKKDPFS KGHICPKAIG LKDIHEDPNR
LKKPLKKVGK NWIEISWDQA INEVSEKLHQ IQEQHGKNAI AIYSGNPSVH NLGTILGAPL
FYKTIKSKNV FSATSADQLA HHLAAATMFG HSNLLPVPDL HRTHHWLILG GNPMVSNGSM
MTAPNARKLI KDIKLKGKVV VIDPRFSETA KKASEHHFIK PASDIWLLLA MIKIILDEKL
ITLNHLENYV STKELSVLKA LLQNLDLDYV AAKTGIKNET ISLITKDFIN AKSASIYGRL
GLSTVEYGSL SIWAINILNI LSGNFDTPGG IMFPKPAIRV VNTKKPVLKF NRWQSTVRKL
PEFNGELPVS TLAEEIFNKK ESKINALITV CGNPVLSTPN GKQLEKAIDS LDFMVSVDIY
LNETTKNADY ILPPATALEV SHYDYIFNNL AIRNTTKYSE PIIAKSKDAL YDFDIFKRLT
ISLLKKHKKT DQTLQQIGMF KNLTLNYLLD SGLKKGCYNL DLEKLKQHPN GIDLGSLKPR
IEDVLLFENK KIRLLSDIYI HEINKLLKSK KTISNTLSLI GRRNLRSNNS WMHNSKSLMK
GSNICNLIIH PNDAMKRNIT SGDLVEITSR VGSVRITADV NDEICESVIS IPHGWGHHRK
GIKLDIAAAN PGVSINDLTD DQFVEELTGV AIFSGIDVEV TLCK
//
