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Database: UniProt
Entry: A0A4Q7KES4_9PSEU
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Original site: A0A4Q7KES4_9PSEU 
ID   A0A4Q7KES4_9PSEU        Unreviewed;       767 AA.
AC   A0A4Q7KES4;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Molybdopterin-dependent oxidoreductase alpha subunit {ECO:0000313|EMBL:RZS31360.1};
GN   ORFNames=EV193_11451 {ECO:0000313|EMBL:RZS31360.1};
OS   Herbihabitans rhizosphaerae.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Herbihabitans.
OX   NCBI_TaxID=1872711 {ECO:0000313|EMBL:RZS31360.1, ECO:0000313|Proteomes:UP000294257};
RN   [1] {ECO:0000313|EMBL:RZS31360.1, ECO:0000313|Proteomes:UP000294257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 101727 {ECO:0000313|EMBL:RZS31360.1,
RC   ECO:0000313|Proteomes:UP000294257};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (FEB-2019) 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:RZS31360.1}.
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DR   EMBL; SGWQ01000014; RZS31360.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Q7KES4; -.
DR   OrthoDB; 5287431at2; -.
DR   Proteomes; UP000294257; 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:UP000294257}.
FT   DOMAIN          121..497
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          649..758
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   767 AA;  83449 MW;  65AB6E2A3E1DFCEC CRC64;
     MSRKPPERDI DESELDVERP KKWAAGIPGV AVSLARSAEQ MGVGRSVRTL RLLNQRDGFD
     CPGCAWPEPR GHRGHVEFCE NGAKAVAEEA TRRRVTPEFF AEHSITELAG KTDYWLGQQG
     RLTHPMVLRD GGTHYEPIDW DDAFTLVADE LRGLASPNEA IFYTSGRTSN EAAFVYQLLV
     RSFGTNNLPD CSNMCHESSG AALVETIGIG KGSVSLADFE LADLILVVGQ NPGTNHPRML
     TALEKAKAAG AKIVAVNPLP EAGLLRFKNP QKVRGVLGKG TALADEFCQI RLGGDQAFFR
     AIGHLLLAWE KAAPGTVVDR ELVDGATGFA AYESTVDDLD WDAVDAATGL DREQIVRVAR
     MIAESKAAIA CWAMGLTQHK HAVATIAEIA NVWLLRGMIG KPGAGLCPVR GHSNVQGDRT
     MGIYEKMPES FLSTLDSEFG ISVPREPGHD TVAAIRAMRD GAGKVFFAVG GNFVAATPDT
     ELTERALRSC ALTVQVSTKL NRSHVVPGRT ALILPTLGRT ERDEQPAGEQ FVTVEDSMSV
     VHRSRGRLAP ASEHLLSEVD ILCRLGTALL GEAHPVPWQA FRTNYDTIRE RIARVIPGCD
     DYNARVREPD GFVLPHPPRD RREFTGTASG KATFAITELD YPRVPEGRLL LQTLRSHDQY
     NTTIYGLDDR YRGVSDGRRV VFVHPDDIAE RGLSDGQLVD LVSEWSTVDG VTERRADKFR
     VVSYSTARGC AAAYFPEANS LVPLDSTADK SGTPTSKSIV VRLEPAG
//
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