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Database: UniProt
Entry: A0A1W1YPV3_9FIRM
LinkDB: A0A1W1YPV3_9FIRM
Original site: A0A1W1YPV3_9FIRM 
ID   A0A1W1YPV3_9FIRM        Unreviewed;       731 AA.
AC   A0A1W1YPV3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Anaerobic selenocysteine-containing dehydrogenase {ECO:0000313|EMBL:SMC37758.1};
GN   ORFNames=SAMN04488500_10232 {ECO:0000313|EMBL:SMC37758.1};
OS   Sporomusa malonica.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Sporomusa.
OX   NCBI_TaxID=112901 {ECO:0000313|EMBL:SMC37758.1, ECO:0000313|Proteomes:UP000192738};
RN   [1] {ECO:0000313|EMBL:SMC37758.1, ECO:0000313|Proteomes:UP000192738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5090 {ECO:0000313|EMBL:SMC37758.1,
RC   ECO:0000313|Proteomes:UP000192738};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; FWXI01000002; SMC37758.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W1YPV3; -.
DR   STRING; 112901.SAMN04488500_10232; -.
DR   OrthoDB; 9759518at2; -.
DR   Proteomes; UP000192738; Unassembled WGS sequence.
DR   GO; GO:0018818; F:acetylene hydratase activity; IEA:InterPro.
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; cd02781; MopB_CT_Acetylene-hydratase; 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   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR037949; MopB_CT_Acetylene-hydratase.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
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; PS00490; MOLYBDOPTERIN_PROK_2; 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:UP000192738}.
FT   DOMAIN          2..58
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   731 AA;  82127 MW;  8AB0620A8A362078 CRC64;
     MSEIRKTACH FCHMNCGMLA TVENGVVTKV VGDPEHPFNQ GAQCPRGVSA LDHLNHPNRI
     NFPLKRVGER GSGQFERVSW EEALDDIAAR LAALKQKYGA ETIATTGGTN RTDDFARRRF
     FNLVGSPNVV HTAPVCWIPN FLTEAASYGW AAFDPEVAGA KCAVIWGHNG GASYLPEMRG
     MLQAKANGTK IIVIDPNYSE TASKADIWLP LKPGSDNALA LAWLNVIINE GLCDYQFIEE
     WTVGFEELCD RVQEYTPEWA AEKTGVSPEL IIETARIYAM SKPACIVWGV ATDQLGKGSA
     ASAQARVALR IICGNLDVPG GDVMPGPHPL FITDWEMELN EMLPEEQRVK QLGSERFKLN
     TWPGYQLLTE NMLRVWGKSI PAEWFCEANP STVFRAMVTE KPYPVKACIT LANNPLVSYA
     NSKLVYEGLK NLDLYVVMEY WMTPAAMLAD YVLPAASWLE RPVMTTTYGV SDWLIASERA
     IEPMFERKTD IEFWSELGHR MGQAEYWPWK TDEEIFKYRL DPLGLELESY EEFVQCYRMH
     FADREYRKFE TRGVATPSGK VELKISIFEQ LGYDPLPHYV APPFSAEAKP ELAQEYPLSL
     VAGGGFMPFF HSEHREITRI RLLRPNPRVA INPTLAQKLN IKEGEWVWIE TPTGKVKQTA
     FITSAVAPDV IQAERGWWFP EKEIKDPSLM GVFESNINVC VDDDPDTLDE LCGSFCSRGI
     MCRISKVEGN D
//
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