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Database: UniProt
Entry: A0A4Q9H115_9BURK
LinkDB: A0A4Q9H115_9BURK
Original site: A0A4Q9H115_9BURK 
ID   A0A4Q9H115_9BURK        Unreviewed;       772 AA.
AC   A0A4Q9H115;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=FdhF/YdeP family oxidoreductase {ECO:0000313|EMBL:TBO27864.1};
GN   ORFNames=EYS42_15620 {ECO:0000313|EMBL:TBO27864.1};
OS   Aquabacterium lacunae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Aquabacterium.
OX   NCBI_TaxID=2528630 {ECO:0000313|EMBL:TBO27864.1, ECO:0000313|Proteomes:UP000292120};
RN   [1] {ECO:0000313|EMBL:TBO27864.1, ECO:0000313|Proteomes:UP000292120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMB7 {ECO:0000313|EMBL:TBO27864.1,
RC   ECO:0000313|Proteomes:UP000292120};
RA   Chen W.-M.;
RT   "Aquabacterium sp. strain KMB7.";
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:TBO27864.1}.
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DR   EMBL; SIXI01000008; TBO27864.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Q9H115; -.
DR   OrthoDB; 5287431at2; -.
DR   Proteomes; UP000292120; 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:UP000292120}.
FT   DOMAIN          109..488
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          654..742
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   772 AA;  84060 MW;  7977B81AF1134E11 CRC64;
     MSQAKIEFYK GPAGGWGALR SVARQLLQHR IAAKGARTLL SANQPDGFDC PGCAWPDRQH
     TSSFEFCENG VKAVAAEATA DRATPELIGQ HTVSALRTWP DHDLEAMGRL TEPLVYRPAT
     DRYERITWDE AFATVARHLR ALASPDEAVF YTSGRTSNEA AFLYQLFVRE FGTNNFPDCS
     NMCHEPSGMG LKASVGVGKG TVTLEDFEHA DCILIFGQNP GTNHPRMLGE LRAAAKRGAR
     ILSFNPLRER GLERFADPQS PVEMLGGGAT AITSDYFQPQ VGGDIAALKG LMKHLLTLDV
     QARAEGRAPV LDDAFIATHT QGFQALKADL LAEPWPLIER ESGLSQAQLH HAAEVIARAQ
     GVIACWGMGI TQHRHGVGAV QMIANLLLMR GMVGRPGAGL CPVRGHSNVQ GDRTMGIDEK
     PTTAFLDRLE RVYGFAPPRH EGFDTIGAIE AMRDGRAHVF FGMGGNFAAA TPDTPATWAA
     LQRCALTVHV ATKFNRSHTV HGREALVLPC LGRTEIDQQA TGPQHVSVED SMSTVHLSAG
     INEPASPHLL SEPMIVARLA EATLPHSRVP WRWLVEDYDR IRDHIERVFD AFQGFNEKVH
     HPGGFRLRNT ASERVWATPS GKAQFAVHAI PQDTAVHEAR DQARQAGHQP ERVFALTTVR
     AHDQYNTTVY GLDDRYRGVF GQRRVVFVNA ADRQALGLAE GAWVDLVGCA AGDTTERVAP
     GFKLVDYDIP TGCVAAYYPE TNGLVPLSSH AIGARTPTSK SVPVTLRPAQ EA
//
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