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Database: UniProt
Entry: A0A2U1TA00_9CORY
LinkDB: A0A2U1TA00_9CORY
Original site: A0A2U1TA00_9CORY 
ID   A0A2U1TA00_9CORY        Unreviewed;       771 AA.
AC   A0A2U1TA00;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=FdhF/YdeP family oxidoreductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DF222_00680 {ECO:0000313|EMBL:PWC02840.1};
OS   Corynebacterium yudongzhengii.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=2080740 {ECO:0000313|EMBL:PWC02840.1, ECO:0000313|Proteomes:UP000244989};
RN   [1] {ECO:0000313|Proteomes:UP000244989}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2189 {ECO:0000313|Proteomes:UP000244989};
RA   Liu S., Wang Z., Li J.;
RL   Submitted (APR-2018) 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:PWC02840.1}.
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DR   EMBL; QEEZ01000001; PWC02840.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U1TA00; -.
DR   Proteomes; UP000244989; 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:UP000244989}.
FT   DOMAIN          123..492
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          643..749
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   771 AA;  85776 MW;  ED57F3520EB3F4CC CRC64;
     MTSPTDHNPV NPVANKYDHP KVGNRTKHAA GLEGVAVSMR HAVPNHGILP LINMNKSGGV
     DCPGCAWPEP EQGDLGIVEF CENGAKAIAE ETTPERADEE FWASYTVEEL REKTDHWLGK
     QGRITTPLLY DRESGDGHYR PISWDDAYDL IAKHLQETPA DEAVYYTSGR ASNEAAYCFG
     LLARRHGTNN LPDCGNLCHE STGAALTQTV GLGKGSVTMK DIETTDLFIS VGQNPGTNHP
     RALTAFHKLK RNGGKMIAVN PIPETGLMKF REPQSIKGTL GLSEKLADDY VQVRLDGDRA
     FFQQLNREVI KRDLIDHNFV EQFVHGYDEV VEHLKSLDPE ELERGSGVPQ KVVEKVADRV
     AKADSIVVGW TLGVTQHKNA VYTIREMVNF LLLTGNIGKP GAGTAPFRGH SNVQGDRTMG
     IWEKMSDTFL QSLQDEFGFD VPREHGMDSV DSFRAMRDGK ARLFFSLGGN IVRVMSDTSA
     MENGFDRQDL TVHLSTKPNG SHAWPGKKAL ILPVKARTDV DMQASGPQIV SAENSAGIVS
     SSEGHRRAND DLNLQSETEI ICRIGERAFG DDFWAPMRDN YDVVRDHIEN TIPGFENYNE
     RVRQPGGFYL PNGPRERIFN TDVKKAKLTV NETNVIDLPK DHLLLSTVRS HDQFNSTIYG
     LDDRYRGVRH GRRVIFVNGE DLRQRGLKDG DMVDIVSVWD DGERRAPNFR VVEYDSAKDC
     ATSYFPECNV LVPLDNTADY SNTPAYKSVV IRLEPLGYTA DELKEREGQP A
//
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