ID   A0A243WJY7_9BACT        Unreviewed;       851 AA.
AC   A0A243WJY7;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=FdhF/YdeP family oxidoreductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BXP70_02595 {ECO:0000313|EMBL:OUJ76176.1};
OS   Hymenobacter crusticola.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1770526 {ECO:0000313|EMBL:OUJ76176.1, ECO:0000313|Proteomes:UP000194873};
RN   [1] {ECO:0000313|EMBL:OUJ76176.1, ECO:0000313|Proteomes:UP000194873}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIMBbqt21 {ECO:0000313|EMBL:OUJ76176.1};
RA   Liang Y., Feng F.;
RT   "A new Hymenobacter.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:OUJ76176.1}.
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DR   EMBL; MTSE01000001; OUJ76176.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A243WJY7; -.
DR   OrthoDB; 9792592at2; -.
DR   Proteomes; UP000194873; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   CDD; cd02787; MopB_CT_ydeP; 1.
DR   CDD; cd02767; MopB_ydeP; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR037951; MopB_CT_YdeP.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR010046; Mopterin_OxRdtse_a_bac.
DR   InterPro; IPR041953; YdeP_MopB.
DR   NCBIfam; TIGR01701; Fdhalpha-like; 1.
DR   PANTHER; PTHR43105:SF4; PROTEIN YDEP; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   PIRSF; PIRSF000144; CbbBc; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 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:UP000194873}.
FT   DOMAIN          186..563
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          720..824
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   851 AA;  94155 MW;  C940DB54FD60EFA5 CRC64;
     MEKSPAQEPD KSGKTSEQTV TNNVPVSGQR PDQGAAPTND HYDNGGKADA DKRIMEAPDT
     LGAKHKYPVL AQPPEEFTGL KLGKPFKTAA GVEAVLKSMQ YSWGEAGLVR GSHALVKLNQ
     KDGFDCSSCA WPDPDDHRSV AEFCENGAKA TASDTDHRTI GPDFFAQHSV ADLSRFTDRD
     LNSAGRITHP MVLRPGTTHY TPISWPEAFR IVADELNALK SPDEAAFYTS GKVPNEPAYA
     YQLFVREFGT NNLPDCSNMC HESSGAALTN TTGLGKGSVT LNDFYEAEVI LIMGQNPGTN
     HPRMLTALQK AKRNGAKIIA VNPLMEAGLN HFKNPQDFMN PLRAIGALVG DGTQITDLWL
     QVRVNGDMAV LRGIMKYLFE AEENNPGQVI DHDFIKEYTA HFDEFKEEIL NTSWEDIEEM
     SGIPRQQLLD AANIIANKKK IITCWAMGLT QQKNAVYSIG EIVNLHLIKG AVGIPGAGLC
     PVRGHSNVQG DRTMGIWERP SPQFLDALEN EFDFAPPREH GLDSVETAKA MYDSRIKVFV
     SFGGNFLSAM PDTEFIAEGM RKQRLTVFIA PKLNRGHLVT GETSLLLPCL VRSEVDNQKT
     GQQFVTCENS MGVVSMSKGI LKPLDGEMLS ETAIVCGIAL TTLEGRTKTD WVAMTENYDV
     IRNHIERTIP GFEKFNEKVR HPGGFYLPNG PRERKFTTDN AKANFTVTEM KKHTLEPGQL
     VLFSLRSHDQ FNTTVYDYND RYRGVYGERR VIFMNPRDMK ERGIKERQLV NITSHFEGQK
     RMAERFVAIP YDTPKGNCGA YYPEMNVLVP VASVADVSNQ PTSKWVVVTV EAVAEMLPEG
     ATKAERIAVP A
//