ID   W0F4S0_9BACT            Unreviewed;       782 AA.
AC   W0F4S0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Molybdopterin oxidoreductase domain-containing protein {ECO:0000259|Pfam:PF00384};
GN   ORFNames=NIASO_16495 {ECO:0000313|EMBL:AHF16321.1};
OS   Niabella soli DSM 19437.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Niabella.
OX   NCBI_TaxID=929713 {ECO:0000313|EMBL:AHF16321.1, ECO:0000313|Proteomes:UP000003586};
RN   [1] {ECO:0000313|EMBL:AHF16321.1, ECO:0000313|Proteomes:UP000003586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19437 {ECO:0000313|Proteomes:UP000003586};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) 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}.
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DR   EMBL; CP007035; AHF16321.1; -; Genomic_DNA.
DR   RefSeq; WP_008587299.1; NZ_CP007035.1.
DR   AlphaFoldDB; W0F4S0; -.
DR   STRING; 929713.NIASO_16495; -.
DR   KEGG; nso:NIASO_16495; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_16_1_10; -.
DR   OrthoDB; 9792592at2; -.
DR   Proteomes; UP000003586; Chromosome.
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   CDD; cd02787; MopB_CT_ydeP; 1.
DR   CDD; cd02767; MopB_ydeP; 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; 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   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:UP000003586}.
FT   DOMAIN          129..505
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
SQ   SEQUENCE   782 AA;  87084 MW;  A866A8CF1C8A45EF CRC64;
     MEKDSNNKHL PDPENPYKLL DLKLTKVEKW AAGVPAVMAA VSDLIGEKTL IRGTRALFKM
     NQVGGFDCPS CAWPDPDDER SPLGEYCENG AKALAEEATT KKITAEFFKE NSVYDLAQLD
     DYSIGKMGRL TEPMYMPQNG THYQPISWDD AFKKIAAHLN ALATPDEAAF YTSGRTSNEA
     SFMYQLFAKE YGTNNMPDCS NMCHETSGTA LRPTIGIGKG TVKLEDFYDT DVIIIIGQNP
     GTNAPRMMSA LEKGKKNGAK IIAINPLPEA GLLGFHNPQQ ISGIIGNGIK LADLYLPVKI
     NGDMALLKAL ELLLLDFEKK SPGEVLDHAF IGEKTTGYEV FLKQFEAYNL EELATASGVS
     AALLYEAAQM MAFKKRIIVC WGMGLTQQPN GVDMIKEILN LLLLKGSIGK PGAGVCPVRG
     HSNVQGNRTM LIDEKPTDEQ LDRLQHFFGF NPPRKHGYDV VRAIKAMQEG KVKFLFCMGG
     NFLSATPDTT YTAQALRKLN LTVFVSTKLN RSHLIHGKEA IILPTLSRSD IDRVNGTHQI
     VSTENSMGVV QSSKGVLKPV SDHLINETQI ACRMAMATLG NKTVVNWQLY HDSYDAVRDA
     IEKCIPGFEN YNVRVRQKDG FYLPNAARDG QFLTKQFGDR APFTLTTVPD NTLAPDEYMM
     ATTRTHDQFN TTIYGLDDRY RGIKNERRVI FMNQKDIDLA GFKAGDKVDL FNYDDGIERI
     APLFIIVAYQ IPERNTVTYF PETNVLVSVN NVVKESNMPA SKYVKIRIKK HDPEIYKRIN
     QL
//