ID   A0A0F7JXH0_9GAMM        Unreviewed;       953 AA.
AC   A0A0F7JXH0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:AKH20372.1};
GN   ORFNames=AAY24_08420 {ECO:0000313|EMBL:AKH20372.1};
OS   Sedimenticola thiotaurini.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Sedimenticola.
OX   NCBI_TaxID=1543721 {ECO:0000313|EMBL:AKH20372.1, ECO:0000313|Proteomes:UP000034410};
RN   [1] {ECO:0000313|EMBL:AKH20372.1, ECO:0000313|Proteomes:UP000034410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SIP-G1 {ECO:0000313|EMBL:AKH20372.1,
RC   ECO:0000313|Proteomes:UP000034410};
RX   PubMed=26089430;
RA   Flood B.E., Jones D.S., Bailey J.V.;
RT   "Complete Genome Sequence of Sedimenticola thiotaurini Strain SIP-G1, a
RT   Polyphosphate- and Polyhydroxyalkanoate-Accumulating Sulfur-Oxidizing
RT   Gammaproteobacterium Isolated from Salt Marsh Sediments.";
RL   Genome Announc. 3:e00671-15(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}.
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DR   EMBL; CP011412; AKH20372.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F7JXH0; -.
DR   KEGG; seds:AAY24_08420; -.
DR   PATRIC; fig|1543721.4.peg.1742; -.
DR   Proteomes; UP000034410; Chromosome.
DR   GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR   GO; GO:0051539; F:4 iron, 4 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   GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR   CDD; cd02750; MopB_Nitrate-R-NarG-like; 1.
DR   Gene3D; 3.40.50.12440; -; 5.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR017840; DMSO_Rdtase_II_Mopterin_su.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   NCBIfam; TIGR03479; DMSO_red_II_alp; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   PANTHER; PTHR43105:SF2; RESPIRATORY NITRATE REDUCTASE 2 ALPHA CHAIN; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 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.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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:UP000034410}.
FT   DOMAIN          79..142
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   953 AA;  107894 MW;  3480B841BB50476F CRC64;
     MRAGVSTTRT GKNVTLGELI MSKYGSTRRG FLKTMGHVSI GMLASGSVVM RTLAQTKDPM
     MQHEYSGWEN YHREQWSWDK KTRGTHLLNC TGSCPHFVYT KNGVVMREEQ SKDIPKLTGV
     PEYNPRGCNK GECAVDYQYG PHRIKYPLIR VGERGEGKWR RVSWDEALEY IANGIVDTIK
     EEASDCISVF TPVPAVAPVS FAAGHRFASL IGGHTHTFFD WYGDHPTGQT QVQGLQGDTC
     ETADWFNGRT ILMWGANSAQ TRIPDAHFLQ EAVLNGSKMY VISPDFNATA TKADVFVGIK
     PGTDAALALG MVNVIVNENL HDIHNLKEQT DLPFLVRKDT KMYLRESDVV EGGSDAKFYT
     WDTKTKKPVL MKGSWGEEPE KKAKLQPGFM GRNTFTFPDG YLDLGDLDPA LEGTYKVKLA
     NGETVKVQPV FEVYKPKLKE YTPEKVSKIT GVAPSVITQM ARDFAKNKPS MIITGGGTNH
     WYWSDTVLRT FILLCAVTGN EGYNGTGVNH YVGQWKPTPL LGVVKLSFPY SPKKHRFCQT
     TLWTYYHGNV YDAMENEGID TAKYLRESIE SGQMPLYPQN GRDPKVFICY RGNWLNNAKG
     LDYVLRNLWP KMNLTVDMNF RMDSTALYSD VVLPSAHWYE KTDLSMTEEH SFIHMTEPAI
     KPMWESKPDW EIFALLAKKV GEVAKKKGFT RYFDEKFNIA RDLTKLYDLQ TDEGKLETDV
     QACQFILDNA PQTAGITLDM IRKEGPQRFK SNWTSPMKEG VPYVPLQNFI IKKKPWPTLT
     GREQFYIDHA TFFEMGVELP VYKAPVDADQ YPLRFNTPHS RYAIHSTWKD NILQLRLQRG
     GPMCEISPAD AKARGIRDND WVEVFNDHGR VIVRCKIRNG EQTGRVSMHH EPELYMDLIG
     DGSSQSPLPV RLNPTALVGN YAHLKFKPNY YGPGGVQRDA RVEVRRYTGS VTV
//