ID A0A0S8D5H4_9BACT Unreviewed; 689 AA.
AC A0A0S8D5H4;
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_02265 {ECO:0000313|EMBL:KPK30810.1};
OS Nitrospira bacterium SG8_3.
OC Bacteria; Nitrospirota; Nitrospiria.
OX NCBI_TaxID=1704023 {ECO:0000313|EMBL:KPK30810.1, ECO:0000313|Proteomes:UP000051394};
RN [1] {ECO:0000313|EMBL:KPK30810.1, ECO:0000313|Proteomes:UP000051394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_3 {ECO:0000313|EMBL:KPK30810.1};
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:KPK30810.1}.
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DR EMBL; LJNR01000022; KPK30810.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8D5H4; -.
DR PATRIC; fig|1704023.3.peg.3989; -.
DR Proteomes; UP000051394; 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}.
FT DOMAIN 2..58
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 689 AA; 77676 MW; E1F3CEC52DCD6075 CRC64;
MERIEKASCG RMDHGGCGLL VHVEEGRVTK IKGDPDSFTR GYVCAKGLAH GERLYHPDRL
VYPQKRVGEK GENQWKRISW AEAFETITEK LLKCKSRSAP EKALFMQGTP RGLENMLLYR
FAHSFGSPNV AATGTVCFAP RLGASILTNG FYPHPDLEHP PELILVWGAN HLATSADGVL
APEVGLTLRR GSRYVLIDPR KSNLASRSEI HLQIKPGRDL LLALGMIKVI IEEELYDREF
VEAWTMGFDA LRAHVKSYTL GEIEEETWTS QEDIRKTSRL YANAGSASIL WGNAIDHTIN
NVQTARALLI LMALSGNLDR PGGNIKASTP KAVRPTEFML TNKYRQISHK MIGADHRLSS
MLGFTPYHLA IKAMLHEDPY KIDFVYVQGT NPLMAYPNAE ETFKGLEKVN FLVVAELFMT
PTAQLADMVL PVATHFEFDD LGYYGQPWGK ILARPKIVEP PGECLSDVKI LNELAMRLGL
EDPFWKDEEA CINYLLGPSG LRFQALKKMG MIEEKKTYEE FKKIGFRTPS GKVELYSSWL
EKNGYPPLPV FSPLENASEE EWDMVLTSAK IHVFFHSMNR NLPSLRRRNP EPTANLHPDT
AKGIGVRQGE WIWVENKQGR AKFKVQLNSG INPSVVFGEH AWWFPERDAA GLYDWKESNI
NMLTENNPPY EPSLGSVNLR GISCRIHKI
//
