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
//