ID A0A0S8CXR6_9BACT Unreviewed; 698 AA.
AC A0A0S8CXR6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Thiosulfate reductase {ECO:0000313|EMBL:KPK27692.1};
GN ORFNames=AMK69_10165 {ECO:0000313|EMBL:KPK27692.1};
OS Nitrospira bacterium SG8_3.
OC Bacteria; Nitrospirota; Nitrospiria.
OX NCBI_TaxID=1704023 {ECO:0000313|EMBL:KPK27692.1, ECO:0000313|Proteomes:UP000051394};
RN [1] {ECO:0000313|EMBL:KPK27692.1, ECO:0000313|Proteomes:UP000051394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_3 {ECO:0000313|EMBL:KPK27692.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPK27692.1}.
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DR EMBL; LJNR01000148; KPK27692.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8CXR6; -.
DR PATRIC; fig|1704023.3.peg.6904; -.
DR Proteomes; UP000051394; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
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; cd02778; MopB_CT_Thiosulfate-R-like; 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 Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 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; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 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; PS00551; MOLYBDOPTERIN_PROK_1; 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}.
FT DOMAIN 2..58
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 698 AA; 78691 MW; 5D3CBAFAE153735F CRC64;
MKESVFSICG MCSVRCPIRV ETEDGLVKWI EGNPHDPGMA GRLCAKGSAG MAMEYDYERP
QHPMIREGRR GEGKWKRATW DEALGYVTAK LKTIIKKHGG KAVALSDRGG PFRDIHRSFL
RAIGSPNYFN HDCTCAQNVQ HAAISLFGSG RKAFNYDYKQ CKHLILYGRN VFESLRVKAA
NTIMELLDRG GKLTYIDIRA SGTAMKATRF WMVRPGTDYA LNLGMIHTIL RDRLYDAEFA
NKWVLGLEAL ESFVSPYTPE WAASETGIPA KELIEFAHEV ADEKPAVIFH PGWMTARYLD
SFYSSRTAYI LNVLMGSLEA PGGLFFTKGP EDVGVRGLNT LLDSIPAPKE KRADGCGWKY
KHFETGPGLL HLLFPAIQSE DPYPIKAYIV FRHDPLLALP DPETQKKVLD KLDLLVAIES
NYSETAWYAD VLLPSATYLE KSSPLATGKG LKPQFRMRKQ AIYPRGEARP DWEIFKLLAQ
RLGVGKYLTF TDMEAFWEWQ LEGTGITVAD LEEKGYVELV DKPIWWDRMK DLKFKTPSGK
IEFVSGRLEE NGIPSLKPYE RPRKPKKGYY RLAFGRSPVH THGRTMNNPV LHEIMPENVL
WINAKEAEQL SIEDNARVKV TSADGNHSGT IRAHVTEFIH PEAVFMVHGF GRKVPWQTRG
FNKGLGDYRF ETGLLDVYDP AGGGIALLEC QVNVKKAE
//
