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Database: UniProt
Entry: A0A316EY01_9BURK
LinkDB: A0A316EY01_9BURK
Original site: A0A316EY01_9BURK 
ID   A0A316EY01_9BURK        Unreviewed;       773 AA.
AC   A0A316EY01;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Molybdopterin-dependent oxidoreductase alpha subunit {ECO:0000313|EMBL:PWK36892.1};
GN   ORFNames=C7419_101762 {ECO:0000313|EMBL:PWK36892.1};
OS   Cupriavidus plantarum.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=942865 {ECO:0000313|EMBL:PWK36892.1, ECO:0000313|Proteomes:UP000245754};
RN   [1] {ECO:0000313|EMBL:PWK36892.1, ECO:0000313|Proteomes:UP000245754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SLV-132 {ECO:0000313|EMBL:PWK36892.1,
RC   ECO:0000313|Proteomes:UP000245754};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT   to study the core and pangenomes of soil and plant-associated
RT   prokaryotes.";
RL   Submitted (MAY-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:PWK36892.1}.
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DR   EMBL; QGGT01000001; PWK36892.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316EY01; -.
DR   Proteomes; UP000245754; Unassembled WGS sequence.
DR   GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
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   GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR   CDD; cd02787; MopB_CT_ydeP; 1.
DR   CDD; cd02767; MopB_ydeP; 1.
DR   Gene3D; 3.40.50.740; -; 2.
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:UP000245754}.
FT   DOMAIN          111..513
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          650..757
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   773 AA;  85641 MW;  AE15A6C78C0692A0 CRC64;
     MSQEKPRIAP YTHAAAGWGA IKYVALSLLR ERVNGLNYRA LFYQNQPHGF DCPGCAWPDR
     EHASTFEFCE NGVKAVAAET TSKRVTREFL AANTVEALMK QTDYELEQHG RLSEPMVYDT
     GTDTYRPIAW QAAFDLIAEH LHALPSPDQA AFYTSGRASN EAAFLYQLFA RAYGTNNFPD
     CSNMCHEATS RGLPFAVGVG KGTVTLRDFE SADTLLLFGQ NPATNHPRML GELRECAKRG
     ATLVSINPLR ERGLERFTNP QSPVEMLTLS STNICSVFVQ PKLGGDFALI KGVAKRVLEL
     DDEAVANNAE RVLDVDFIAT HTRGFEAFAD DLRGESWATI ETESGVARED IEGLALIYAR
     GKRVICTWGM GLTQHKHSVQ TIQLLANLMM MRGNIGREGA GLCPIRGHSN VQGNRTVGIE
     EKPTQAFLDR LGSVFDFEPP REHGYDVVET IEAMREGKVK VFIALGGNFA MASPDSDATW
     DALRSCDLTV HIATKLNRSH LIHGKAALIL PTLGRTEIDM QGGVPQGVTV EDSVSMVHIS
     YGMKQPATQT LMSETAIVAN MACATLGEDK IAWRWYAQDY SRIRDKIEAV IDGFEQYNER
     IAHPGGFHMR VAAREREWDT ASGKAEFLVN PLVVDTPIRR AQARFGERAM VLMTTRSHDQ
     YNTTIYALDD RYRGVFGQRR VVFIHRDDLA MLGFRPGEWV DITTVWDDGV ERRAPGFLLV
     EYNIPRGCIG AYYPETNPLV PLDSVADVCN TPTSKSIPVL LHRTAAPVVS AVS
//
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