ID   A0A2S4MBW2_9BURK        Unreviewed;       775 AA.
AC   A0A2S4MBW2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Molybdopterin-dependent oxidoreductase alpha subunit {ECO:0000313|EMBL:POR52099.1};
GN   ORFNames=B0G62_10567 {ECO:0000313|EMBL:POR52099.1};
OS   Paraburkholderia eburnea.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1189126 {ECO:0000313|EMBL:POR52099.1, ECO:0000313|Proteomes:UP000237381};
RN   [1] {ECO:0000313|EMBL:POR52099.1, ECO:0000313|Proteomes:UP000237381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 18070 {ECO:0000313|EMBL:POR52099.1,
RC   ECO:0000313|Proteomes:UP000237381};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JAN-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:POR52099.1}.
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DR   EMBL; PQGA01000005; POR52099.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S4MBW2; -.
DR   OrthoDB; 5287431at2; -.
DR   Proteomes; UP000237381; 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; -; 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:UP000237381}.
FT   DOMAIN          113..496
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          653..758
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   775 AA;  86130 MW;  32AE06BB94D0DDF3 CRC64;
     MDKLKPKGKI EAYHHPAAGW GALKYVAINL IKERVSGGNY RTLFKQNQPD GFDCPGCAWP
     DREHASTFEF CENGVKAVAA EATTKRVTPA FFAANTVESL MKQTDYELEQ HGRLTDPMVY
     DALTDRYKPI AWDDAFALIA KHLKALESPD EAAFYTSGRA SNEAAFLYQL FVRMYGTNNF
     PDCSNMCHEA TSRGLPTTVG IGKGTVTLED FEIADTIIIF GQNPATNHPR MLGELREASR
     RGATIVSVNP LRERGLERFT SPQHPLEMIT FGSTKIASTF IQPKLGGDFA LIKGVAKRLI
     ELDDEALANG TERVIDLDFI QQHTMGFNAF AEDLRNESWP LLETESGVAR EDIEGLARIY
     ANGKRVIATW GMGITQHKHS VQTVHMLSNL LLMRGNIGRE GAGLCPVRGH SNVQGNRTVG
     IEEKPSQAFL DRLGKVFNFE PPREHGLDVV ETVEHMIEGE VKVFMGLGGN FAMATPDTLR
     TFDGLRSCRL TVHITTKLNR SHLVHGENAL ILPTLGRTEI DVQNGIAQGV SVEDSMSMVH
     ISYGMNKPAS PNLMSETAII AHVAHATLGD DKVDWLAYAG DYAKIRDAIE QTVEGFDQYN
     ERIQHPGGFH LRVASRERDW KTDTGKANFM VHPVQQDTPI ARAKAQHGER LMTLMTTRSH
     DQYNTTIYAL DDRYRGVFGQ RRVVFINPAD IAMLGFKNGD WVDMTTVWDD GVERRADHFR
     LVEYDIPRGC IGAYYPETNP LVPLKSVGDV CNTPTSKSIP VLLHASSEPL ELPAF
//