ID A0A0S8CWQ0_9BACT Unreviewed; 713 AA.
AC A0A0S8CWQ0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=4Fe-4S Mo/W bis-MGD-type domain-containing protein {ECO:0000259|PROSITE:PS51669};
GN ORFNames=AMK69_10635 {ECO:0000313|EMBL:KPK27340.1};
OS Nitrospira bacterium SG8_3.
OC Bacteria; Nitrospirota; Nitrospiria.
OX NCBI_TaxID=1704023 {ECO:0000313|EMBL:KPK27340.1, ECO:0000313|Proteomes:UP000051394};
RN [1] {ECO:0000313|EMBL:KPK27340.1, ECO:0000313|Proteomes:UP000051394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_3 {ECO:0000313|EMBL:KPK27340.1};
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 -!- 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:KPK27340.1}.
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DR EMBL; LJNR01000159; KPK27340.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8CWQ0; -.
DR PATRIC; fig|1704023.3.peg.63; -.
DR Proteomes; UP000051394; Unassembled WGS sequence.
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 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 PANTHER; PTHR43742:SF3; DIMETHYL SULFOXIDE REDUCTASE DMSA; 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; PS00932; MOLYBDOPTERIN_PROK_3; 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 11..67
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 713 AA; 79078 MW; C6563DC5C9E86018 CRC64;
MKQKRDPIGQ DEVITTCCSY DCGGRCLLRV HISAGRIKRI STDRGTGPGL RACVRGLSQR
DVAYAPDRLS KPLKRTGERG SAKFVPISWE EALEKVSREL ERVKEQYGVH SIFLMDYYGS
LSPLHGTLKS ARRFFSLFGG CTTTWGSTSL EAAHFASLAT FGTPFTGNSR DNLLHSRLII
MWGWNPLVSR FGPDTVSYLA LAKKAGAKII CVDPRRSQSA KALAEEWIAI RPGTDTALLL
AMAHVMITEE IYDHHFIETY TMGFEKFKDY LTGKEDNLPK TPMWAEEITG VAAQRIRKLA
MDYATLRPAA LWASWAPGRS AFGEQYHRAA MTLAAMTGNM GITGGHLAGG TEYVPLGSLG
ESFPIPKKKN PTVHVSKVFD ALIQGKSGGY PSDIKLLYVV GSNFLNQFSN TNRGVAALKR
PQFIVVHELF LTPTARYADI ILPVTHFFEK EDVGQPWLGG PYFIYMNKVL DPLPEAKSDL
EIFSELARRL GIPSYNDKSE EAWIREFVAS TPELPGYEAF KKKGVHRIEL DQPYVAFRKQ
IEDPAQYSFP TPSGKMEIYS QKLAEMNNPL LPPIPKYLEP WEGPKDPNAD RYPIQLVSPH
SKARVNSTLD NIPRLKSLAD DALWINPIDA QPRGIRNGDK VRVFNDRGEL LTTAKVTERI
MPGAASLDAG AWFRPDDKGL DHGGCVNILT KDEMSPGGAF ASNSCLVQVT LAS
//
