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Database: UniProt
Entry: A0A177YJY3_9NOCA
LinkDB: A0A177YJY3_9NOCA
Original site: A0A177YJY3_9NOCA 
ID   A0A177YJY3_9NOCA        Unreviewed;       791 AA.
AC   A0A177YJY3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Molybdopterin oxidoreductase domain-containing protein {ECO:0000259|Pfam:PF00384};
GN   ORFNames=A3K89_19490 {ECO:0000313|EMBL:OAK55539.1};
OS   Rhodococcus kyotonensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=398843 {ECO:0000313|EMBL:OAK55539.1, ECO:0000313|Proteomes:UP000077519};
RN   [1] {ECO:0000313|EMBL:OAK55539.1, ECO:0000313|Proteomes:UP000077519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KB10 {ECO:0000313|EMBL:OAK55539.1,
RC   ECO:0000313|Proteomes:UP000077519};
RA   Jeong H., Hong C.E., Jo S.H., Park J.M.;
RT   "Genome sequence of Rhodococcus kyotonensis KB10.";
RL   Submitted (MAR-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}.
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:OAK55539.1}.
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DR   EMBL; LVHI01000009; OAK55539.1; -; Genomic_DNA.
DR   RefSeq; WP_068423519.1; NZ_LVHI01000009.1.
DR   AlphaFoldDB; A0A177YJY3; -.
DR   Proteomes; UP000077519; 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   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:UP000077519}.
FT   DOMAIN          123..519
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   REGION          765..791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        771..785
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   791 AA;  86903 MW;  60C060E93E2E2A33 CRC64;
     MRAGKHDVRD YDEADLDIEK PKTHAAGATA VAVSMKRALG HMGPVRTAKT LLDLNQAEGF
     DCMSCAWPDP DPGHRHVAEF CENGAKAVAE EGTTTRATPD FFAAHSIADL DSRTEHWLGQ
     QGRITHPMVK LPGARYYEPI EWDDAFRLIG DQLMSLADPT EAIFYTSGRA SNESAFVYQL
     FARAFGTNNL PDCSNMCHES TSIALQESIG IGKASVTLED VYAAELIVIA GQNPGTNHPR
     MLSALEKAKQ NGAKILSINP LREAGLVNFK NPQTPRGMVG PGTDISDMHL PIKVNGDLAL
     FQAFGSLLVE WDCIDHDFID RHTNGYEDWK AHVTAVDWDV VTSSTGLTRE QITDAAKMLR
     DSKATVFCWA MGLTQHRNAV ATIKEVTNLA FAQGNIGKKG AGLFPVRGHS NVQGDRTMGI
     WERVPQHFLD SIQKEFGFDP PREHGHDTVD SIRAMRDGKA QFFLGLGGNF VQATPDTDVT
     AQAMRNLAMT VHISTKINRS HLVTGDTALI LPTLGRTEKD VQATGPQWIS VEDSTCSVHS
     SRGPLKPASE HLRSEVAILT GIAEAAIGDR YGIDWKGMRD DYRLIREHIS RVVPGCAGYE
     VNVRRPGGFI LPHPPRDSRT FETDSGKGEF VASPIEVLHV PDGHLLLQTL RSHDQFNTTI
     YGLSDRYRGI EGGRRVVFLH RDDIAALGFQ DGDFVDLVTR WEDDDIERCA SNFRIVEYDT
     PRGCAAAYYP ETNPLVPLDS TAMESNCPTS KSVVIQVVRA GTACEPVGHG HQDDTGSDWS
     HKTHPQPHHL S
//
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