ID V5TLJ1_HALHI Unreviewed; 831 AA.
AC V5TLJ1;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Dimethylsulfoxide reductase {ECO:0000313|EMBL:AHB66176.1};
GN ORFNames=HISP_09230 {ECO:0000313|EMBL:AHB66176.1};
OS Haloarcula hispanica N601.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=1417673 {ECO:0000313|Proteomes:UP000018572};
RN [1] {ECO:0000313|EMBL:AHB66176.1, ECO:0000313|Proteomes:UP000018572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N601 {ECO:0000313|EMBL:AHB66176.1,
RC ECO:0000313|Proteomes:UP000018572};
RX PubMed=24625874;
RA Ding J.Y., Chiang P.W., Hong M.J., Dyall-Smith M., Tang S.L.;
RT "Complete Genome Sequence of the Extremely Halophilic Archaeon Haloarcula
RT hispanica Strain N601.";
RL Genome Announc. 2:e00178-14(2014).
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP006884; AHB66176.1; -; Genomic_DNA.
DR RefSeq; WP_014040610.1; NC_023013.1.
DR AlphaFoldDB; V5TLJ1; -.
DR GeneID; 23804818; -.
DR KEGG; hhn:HISP_09230; -.
DR HOGENOM; CLU_000422_13_3_2; -.
DR Proteomes; UP000018572; Chromosome 1.
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:UniProtKB-KW.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 2.
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 InterPro; IPR006311; TAT_signal.
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; PS51318; TAT; 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 Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 56..113
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 803..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 92437 MW; D158029921F1921E CRC64;
MTDDDGVYRR DVLKASGAAA ALGLGGGEFF QTLVESGDGT GPSNRDSGIE SYVGQNEVIQ
TVCSPNCRGK CPIDVHVRDG QVKKVEPHPP EDEQYKRACV LGLSHTQRVY DPTRLKYPMK
RTDWSPDEPN PDGRGPDAEF ERVSWDEALD LVADKMQSLK ADFGPESVLF HVGFGNYGQS
GTAFSRLASL FGSTQPASTI DTNVGRGFNR VTGTGFYLPS TNEAEDWENA NTIIVWGSDL
FSSQFQMDAS EVLDAVENGA KLVVVDPVYT TTASKADLWL PVKPGKDVHL ALAMMHTVFE
DGTYDEQFLR QRTTGPALVR KDTGDLLKSS TVFDDGSDDQ VVAVEQGSNT AVELEPETDG
PYALFGEFTV DGIECETALT RLRDHVADYA PSEVAEQTGV DAENIRTAVR WLATRGPGGI
APSYALGRYK HGHIFGQTYA MLMGLTGDYG RHGNIHAHHS GGATLSTGGW STPEDADPGP
SVRFSDYPDA MIDGDPHKVR AVYSIESNMM GNQFPDRQRF REAIKSLEMF VVADMHHTDT
VQHADIIFPV PHWFEQEDIV SSWGSHPHIS YRHKVQEPMW EARDDYYAIR GLAERLGFGD
YFPETKRELL RELASRDDAI DFETLSEQGT QKKQNIPIVK FTDAFPTDTG RIKMYDDDAP
SEEGVTFDLP RPLEDRTADD YEKADEYPLM FMQKHSRFRI HSQYEMLNWV REVNPEPQLD
IHPSDAKARG IEDGEYVRVH NDRGEMIVKA KYNEAFQPGL VNTDQGWWSR DYVAGHHNDL
THNEVSEVGQ TMAFYDVRVE VEPAPDDVDT DKYEADNPRG AGADAPRAGG D
//