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Database: UniProt
Entry: E6W5S3_DESIS
LinkDB: E6W5S3_DESIS
Original site: E6W5S3_DESIS 
ID   E6W5S3_DESIS            Unreviewed;      1009 AA.
AC   E6W5S3;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   SubName: Full=Molybdopterin dinucleotide-binding region {ECO:0000313|EMBL:ADU67208.1};
GN   OrderedLocusNames=Selin_2495 {ECO:0000313|EMBL:ADU67208.1};
OS   Desulfurispirillum indicum (strain ATCC BAA-1389 / DSM 22839 / S5).
OC   Bacteria; Chrysiogenota; Chrysiogenetes; Chrysiogenales; Chrysiogenaceae;
OC   Desulfurispirillum.
OX   NCBI_TaxID=653733 {ECO:0000313|EMBL:ADU67208.1, ECO:0000313|Proteomes:UP000002572};
RN   [1] {ECO:0000313|EMBL:ADU67208.1, ECO:0000313|Proteomes:UP000002572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1389 / DSM 22839 / S5
RC   {ECO:0000313|Proteomes:UP000002572};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Haggblom M., Rauschenbach I.,
RA   Bini E., Woyke T.;
RT   "Complete sequence of Desulfurispirillum indicum S5.";
RL   Submitted (DEC-2010) 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; CP002432; ADU67208.1; -; Genomic_DNA.
DR   RefSeq; WP_013507079.1; NC_014836.1.
DR   AlphaFoldDB; E6W5S3; -.
DR   STRING; 653733.Selin_2495; -.
DR   KEGG; din:Selin_2495; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_008235_0_0_0; -.
DR   InParanoid; E6W5S3; -.
DR   OMA; ERYSGCP; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000002572; Chromosome.
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   CDD; cd02758; MopB_Tetrathionate-Ra; 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; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR041929; Tetrathionate-R_A_N.
DR   PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 1.
DR   PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000002572};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          68..154
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   1009 AA;  110973 MW;  1202F42F76F38821 CRC64;
     MEKNRRQFLL GTAAVAGLGA VAGYSETLSS VVTLGDKGER MADPVYGQAE EPEFTIDSDG
     KAQPNPRYRV AASVCNGCTT HCGVRVKIDR ETNQVVRVSG NPYNLLSSDP WLPYQTPLGE
     SFTRTSGFQE QGNANRSTAC ARGNMVFDKL NDPFRVLRPL KRVGKRGEDK WEPISVEQLM
     REIVEGGDLF GEGHVDGLRA LRDIETPIDA GNPEMGPKAN QLAIFGTGDE GRQAFIVQRF
     AQSFGTPNFF GHTSICGLSM RAGEAAFLSG LGADPHLKPD FEECEFLLTI GTSPAQAGNP
     FKRQAKLLAR ARSDKNLKYV VVGPMLTNCD SIACGERSRW LPIKPGEDLA LVMGMIRWIV
     ENDRHNAHYL GIPSQQAMQA AGEPSFTNAS HLVVQSGERQ GHILKDGDDA LVIDERDGAL
     KKASEVLQAR LEVDGEVQWQ GHRYQVKSAF TLMKEAAQEH TLEEYSRFCG VPVNDIIDLA
     REFTSHGRKA AIDCHGGTMH TTGYYTTYAI MMLGALIGNL NYRGGMSVGG GKFRDFNGAA
     YNLVGYAGKV QPRGYRADRA RRAYENTKEY RDRVAAGQNP YPARDTWYPF ARALESEVIV
     SSIKEYPYKL KALISWNANF IYGQSGIEHL LDDLKDPQRS IPLIIAIDPF INESSRYADY
     IIPDAVLYET WGVVRPWNGY LTRANNFRYP VLPAPQERFA NGEPITMDSF VIELGKYMGL
     PGFGPGAING TDGKKYAMDR PEDFYLRAFE NVALDGQPVP DISDEEIRLA GLEGYVDTLK
     RVNGENWRKV AYCMARGGRY DGKERAYNGA VLGQTYKQPI SVYSEQVGNH RNSLTGEKFS
     GVPRYFPQSY TDGTPLSSSF DPQKFSLRAF SYKSSVLSQA VAASDAITQL RYTTYVDLNP
     ATARKLGLQH GDEVEVQSPA AAIRGLLRLR QGVHPEAVAI EHGAGREGEG AITLTVGGQT
     LKGRINRKSG LNINKLGLTD QSRDGVATLA DIVVGSNARQ AIPVRVSRV
//
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