ID   A0A1I0RYM1_9BACT        Unreviewed;       768 AA.
AC   A0A1I0RYM1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Oxidoreductase alpha (Molybdopterin) subunit {ECO:0000313|EMBL:SEW46698.1};
GN   ORFNames=SAMN05428988_6477 {ECO:0000313|EMBL:SEW46698.1};
OS   Chitinophaga sp. YR573.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=1881040 {ECO:0000313|EMBL:SEW46698.1, ECO:0000313|Proteomes:UP000198758};
RN   [1] {ECO:0000313|EMBL:SEW46698.1, ECO:0000313|Proteomes:UP000198758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR573 {ECO:0000313|EMBL:SEW46698.1,
RC   ECO:0000313|Proteomes:UP000198758};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOJF01000003; SEW46698.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0RYM1; -.
DR   STRING; 1881040.SAMN05428988_6477; -.
DR   OrthoDB; 9792592at2; -.
DR   Proteomes; UP000198758; 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; 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}.
FT   DOMAIN          136..503
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          654..758
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   768 AA;  84272 MW;  A97A3DFEBB557EDF CRC64;
     MAKASIVPNA ENPEKFTGDL RLGKPKTTAA GIPAVISSAK HILEEMDAAR GFKALIKLNQ
     KDGFDCPGCA WPDPDDDRSS LGEYCENGAK AVAEEATSKK LTASFFAENS VAGLAELTDF
     EIGKKGRVAE PVYLPEGATH YQPISWEKAF KKIAGHLNAL SSPNEAIFYT SGRTSNEAAY
     LYQLFVREYG TNNMPDCSNM CHESSGVALG ESLGIGKGSV TLDDLYMAEV IIVLGQNPGT
     NHPRMLSALQ KAKANGATII AVNPLHETGL LNFLNPQTVK GFLNIKTHLT DIFLQVKING
     DLALLKALTL LLLQEEDKHP GTVFDAEFIA ADTLGYAEYI AHLRQQDLSQ LVIDCGVPLE
     QIELAAKAIM HKKKIITCWA MGLTQHKNAV DTIKEVVNLL LLKGSIGKPG AGTCPVRGHS
     NVQGDRTMGI FERPSEQLLN AIQKVYGFEP PREHGFDTVS AIKAMRDGKG KVFFAMGGNF
     LSATPDTEVT AQALRNCDLT VHVSTKLNRS HLVHGKEAII LPCYGRSDED IINGEKQFVT
     CENSMGVVQM SKGNLKPVSE HLLSEPAIVC QLAQATLGSK SLVNWERYSQ HYDHIREDIE
     KVIPGFDNYN ERVRHPGGFY LPNGAREGRF NTKTGKAHFN VADVTTQQLA ADEFMMMTIR
     SHDQFNTTIY GLDDRYRGIY QERRVILMNI KDIISAGLQP GDVVDLYNEF GGTERVVHKF
     IVVEYNIPEK CTATYFPETN ALVPLNSVAD KSNTPTSKLV ILKIKKST
//