ID A0A1I0QUN6_9RHOB Unreviewed; 943 AA.
AC A0A1I0QUN6;
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:SEW30683.1};
GN ORFNames=SAMN04488515_2172 {ECO:0000313|EMBL:SEW30683.1};
OS Cognatiyoonia koreensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cognatiyoonia.
OX NCBI_TaxID=364200 {ECO:0000313|EMBL:SEW30683.1, ECO:0000313|Proteomes:UP000199167};
RN [1] {ECO:0000313|EMBL:SEW30683.1, ECO:0000313|Proteomes:UP000199167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17925 {ECO:0000313|EMBL:SEW30683.1,
RC ECO:0000313|Proteomes:UP000199167};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; FOIZ01000001; SEW30683.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0QUN6; -.
DR STRING; 364200.SAMN04488515_2172; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000199167; 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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02783; MopB_CT_2; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR PANTHER; PTHR43598:SF5; DMSO REDUCTASE CHAIN A; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 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 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000199167}.
FT DOMAIN 16..72
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 915..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 943 AA; 104618 MW; 220A678F84CB120F CRC64;
MSLDQPAIDL SPRVSDEVRK TTCYMCACRC GINVHMKDGK VAYIEGNKDH PVNKGVLCAK
GSAGIMQHNA PSRLRAPLKR VGERGSGEYE EISWEEALTL ATEWLAPIRA NAPEKLAFFT
GRDQSQSFTS LWAQGFGTPN YAAHGGFCSV NMAAAGIYTM GGAFWEFGQP DWDRTKMVMI
FGVAEDHDSN PIKMGIGRAK ARGAKIVGVN PIRTGYNAVA DDWVGITPGT DGLFILSMIH
CLMKAGKIDL DYLARFTNAS VLINEDPKSD QRGQFLRDDQ GQPLVIDRAT GKLAPWNGVG
VEPDLSKTHR AKGITHRPAF HLMAEKYMSD DYAPEAVADR CGLTPARIRQ MAAELARVAF
DEAITVDQPW TDFRGKHHDR MIGRPVSFHA MRGISAHSNG FQTCRALHVL QIILGSVETP
GGMRFKPPYP KPATAHPKPH GKVTPGQALD GPHLGYVHGP EDLLLDENDQ PKRIDKAYSW
ENPMSAHGLM HMVISNAHAG TPYKIDTLFM YMANMSWNSS MNTGGVMKML TDKDEDGEYV
IPRIIYSDAY SSEMIAYADL ILPDTTYLER HDCISLLDRP ICEADAVADA IRWPVVEPDR
DVRGFQSVLC ELGARLGLPG FVNEDGSQKY ADYADYITHH IRRPGIGPLA GFRLGENGKM
QGGRGDVNEA QLDNYISNGG FWMEHVPAEC SYYKPFNAAY QDWAVKLGFY DVVQPYIFQI
YCEPLRKFQA AAEGIGTRQP PEHLRDQIKA TMDPLPIWYA PFEDSSVDPD EYPIHALTQR
PMAMYHSWGT QNAWLRQIHG HNPLYLPTAI WEQHGFAEGD WAKVTSAHGS IVVPVAHQAS
LNAHTIWTWN AIGKRKGAWA LDTDASEANK GFLLNHLIHE LLPPKGDGLR WANSDPITGQ
AAWFDLRVKI EKTRETNEAK PAMPPLKSPV PQGPETLVWK VGT
//
