ID   F8J7U9_HYPSM            Unreviewed;       675 AA.
AC   F8J7U9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Putative molybdopterin oxidoreductase {ECO:0000313|EMBL:CCB64758.1};
GN   OrderedLocusNames=HYPMC_1528 {ECO:0000313|EMBL:CCB64758.1};
OS   Hyphomicrobium sp. (strain MC1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Hyphomicrobiaceae; Hyphomicrobium.
OX   NCBI_TaxID=717785 {ECO:0000313|EMBL:CCB64758.1, ECO:0000313|Proteomes:UP000000494};
RN   [1] {ECO:0000313|Proteomes:UP000000494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC1 {ECO:0000313|Proteomes:UP000000494};
RA   Genoscope.;
RT   "The complete genome of Hyphomicrobium sp. MC1.";
RL   Submitted (MAY-2011) 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; FQ859181; CCB64758.1; -; Genomic_DNA.
DR   RefSeq; WP_013947165.1; NC_015717.1.
DR   AlphaFoldDB; F8J7U9; -.
DR   STRING; 717785.HYPMC_1528; -.
DR   KEGG; hmc:HYPMC_1528; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_5; -.
DR   Proteomes; UP000000494; 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: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   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.
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   Reference proteome {ECO:0000313|Proteomes:UP000000494}.
FT   DOMAIN          4..61
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   675 AA;  71881 MW;  F78400521AAB151B CRC64;
     MATQAIVKTT CPRDCYDACG MIVKMASDGA VSVVGDPDHD MSRGKLCGKC SIAYNGVWRS
     KTDRLTTPLK RVGPKGSGQF AEVSWDDAIS EIAQRLQSII ATDGGQAILQ THYTGTCSLI
     AGLFPLRFFN RIGATEVDPD TVCNKAGHVA LQLAFGESTR GFDPRTVSSS KCVLIWGANP
     SASAPHVHEH WVARSGVPTI VVDPIRHATA EAADIHLQLF PGTDAALAFA MLAVIKSAGK
     LDRDFLARHC IGWDDIEPQL DACTLSWAEA TTGVPASLIE KAALLYADGP SLLWMGQGFQ
     RQTFGGNAMR SVGLLPPATG NIGKLGAGFL YLNGWDARGV DGGYLSASHL NADPQSVSHM
     DLAARLESGE TKALFTWNNN IAASSPEQAR LRQALRREDL LQVTVDLFQT DTADYADFVL
     PAASFLEFDD VVMSYFTHSV SAQVAALPPL GDALPNQEIF RRLAAAMGLT DPELRETDGV
     IIETILSQAR PGLDFKTLAA AGTMYVPEDP NVQFASHDYR TPSGKIEMTG AQFVEAGLPS
     APAPLSERRP ALGEYRMLSP ASEWLMNSSY ANDGKIARRL QMCEAWLNPS DAETIGVESG
     NRLQVSSKTG SIELSVGISS AVPAGVLLAP KGQWPKASAS GANINVLNPG EKADLAQSCA
     VHSINVTLAK SQIAT
//