ID A0A1H9FEN5_9RHOB Unreviewed; 927 AA.
AC A0A1H9FEN5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Anaerobic selenocysteine-containing dehydrogenase {ECO:0000313|EMBL:SEQ35923.1};
GN ORFNames=SAMN04488092_10649 {ECO:0000313|EMBL:SEQ35923.1};
OS Thalassovita taeanensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Thalassovita.
OX NCBI_TaxID=657014 {ECO:0000313|EMBL:SEQ35923.1, ECO:0000313|Proteomes:UP000198634};
RN [1] {ECO:0000313|EMBL:SEQ35923.1, ECO:0000313|Proteomes:UP000198634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22007 {ECO:0000313|EMBL:SEQ35923.1,
RC ECO:0000313|Proteomes:UP000198634};
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; FOEP01000006; SEQ35923.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9FEN5; -.
DR STRING; 657014.SAMN04488092_10649; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000198634; 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:InterPro.
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 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:UP000198634}.
FT DOMAIN 16..72
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 421..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..927
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 927 AA; 102481 MW; 586BE0BA49EFD821 CRC64;
MTHPRPHLDT SPKVSDEVRK TTCYMCACRC GINVHLKDGK VAYIEGNRDH PVNKGVLCAK
GSAGIMQVNA PSRLRAPLKR TGPRGSGQFA EISWDEALEL ATSWLRPLRE TAPEKLAFFT
GRDQSQSFTG LWAQQFGTPN FAAHGGFCSV NMAAAGIYTM GGAFWEFGQP DWDHTKLFIL
FGVAEDHDSN PIKMGLGKIK ARGARVIGVN PIRTGYNAVA DDWVGITPGT DGLLILSLVH
ELLRAGKIDL DYLARYTNAP VLLDTDTGLF LRDADGKPLV IDRNTGLPAA FDQKSIHPDL
GAIHTVDGKT HRPVFHTLAE RYLDPQYAPE AVAERCGLSP NKIKRLAAEI ARVAFDEAIS
LPIAWTDFRG ERHSHMTGRP VAFHAMRGIS AHANGFQTAR ALHMLQILLG TVETPGGFRF
KPPYPKPAEA HPRPHFKTTP GQPLDGPHLG YPQGPADLCL DDNGQPARID KAFTWDNPLS
AHGLMHMVIS NAHAGDPYKI DTLFLYMANM AWNSSMNTAG VMQMLTDTDA SGDYVIPHII
YSDAYSSEMT AYADLILPDT TYLERHDCIS LLDRPISEAD AAADAIRWPV ITPDRDVRGF
QSVLIDLAHR LKFPAFTNAD GGAKYQDYAD YIVTHERKPG IGPLAGWRGD GSQTGRGAPN
PEQLQRYIDN GGFFVSHIPE TASYYKPWNM AYQDWAVGMG LMDQPTPYLF QLYVEPLRQF
QRAAEGHGAH QPPEHLRPQI RERLDPLPIW YASADSDCAE YPVHALTQRP MAMYHSWGSQ
NAWLRQIHGH NPLYIPTKLW QQHGFQDGDW ARVTSPHSSI TVPVAHMAAL NENTVWTWNA
IGKRKGAWAL KPDAPEATKG FLLNHLIAEL LPPKGDGLRW SNSDPITGQA AWFDLRVRIE
RTAPPTEAHP SFPPLTSPVG TGPKDPK
//