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
//