ID A0A1H9PQT2_9PSEU Unreviewed; 706 AA.
AC A0A1H9PQT2;
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:SER50601.1};
GN ORFNames=SAMN04488000_109221 {ECO:0000313|EMBL:SER50601.1};
OS Lentzea albida.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=65499 {ECO:0000313|EMBL:SER50601.1, ECO:0000313|Proteomes:UP000199503};
RN [1] {ECO:0000313|EMBL:SER50601.1, ECO:0000313|Proteomes:UP000199503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44437 {ECO:0000313|EMBL:SER50601.1,
RC ECO:0000313|Proteomes:UP000199503};
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; FOFV01000009; SER50601.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9PQT2; -.
DR STRING; 65499.SAMN04488000_109221; -.
DR Proteomes; UP000199503; 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 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 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}.
FT DOMAIN 13..70
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 706 AA; 76467 MW; 0916C6EC22305AAA CRC64;
MPRQNLLTIT GTTSEVAGAC PLDCPDCCSW LVTVENGLAT GLRGNPEHPI TRGTLCVKVN
RYLEQASHRD RILHPMRRVG AKGEGRFARI GWDEALDEMA DRLSRIADEH GGEALWPYQG
TGALGYLQGV QGRAGTRLWN VLGASHHDMT ICSIAGLTGL TYALGTSRGM DPEDFALSKL
TLLWGTNTLT SGHHLWRFIE AGRKNGGHVV AIDPMRTRTA AAADEHLAPM PGTDGALALG
LMHVIVATGR EDDDFLSRYC FGWEDFRERV LAFTPERAAS ITGVLAEQIR DLGERIACTK
PTAIRTSQGI QRHAGAGATL RTLACIPAVT GDWHRPGGGL MFSTDTYFGG NREALFRDDL
RPKAVRTLSM TRLAEGLLEA SDPPVMGLVV YGANPVVSTS DQNRVRAGLS REDLYTVVID
HFPTDTVDYA DLVLPATMQH EHTDLMDAYG HLYLAWNERA VEPPGECRST TDTFRDLAKR
MGLREPSLYD SDERLAEQLL DSDHPSLHGI TLDGLRASGW ARLNYPSPLA PFEHGFPTPS
GKFEFVSASA AADGLDPMPG YTPPLEVVDD EMAERHPFVL IAGASHFAIN TIFGNNDELR
RRAGSPTVVV HPDDALAHGL ATGTHVRVFN GRGEFTADVL VDARVRRGVL STTKGHWLKL
TGGATVNATV DERDADMGGG AVFHDNRVSV EAVEIPAAQI RGGAST
//