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Database: UniProt
Entry: A0A0P9F840_RHOGW
LinkDB: A0A0P9F840_RHOGW
Original site: A0A0P9F840_RHOGW 
ID   A0A0P9F840_RHOGW        Unreviewed;       916 AA.
AC   A0A0P9F840;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=4Fe-4S Mo/W bis-MGD-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=RHOBADRAFT_30761 {ECO:0000313|EMBL:KPV71838.1};
OS   Rhodotorula graminis (strain WP1).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV71838.1, ECO:0000313|Proteomes:UP000053890};
RN   [1] {ECO:0000313|EMBL:KPV71838.1, ECO:0000313|Proteomes:UP000053890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP1 {ECO:0000313|EMBL:KPV71838.1,
RC   ECO:0000313|Proteomes:UP000053890};
RX   PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA   Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA   Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT   "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT   graminis WP1.";
RL   Front. Microbiol. 6:978-978(2015).
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC   -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. NasA/NapA/NarB subfamily.
CC       {ECO:0000256|ARBA:ARBA00008747}.
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DR   EMBL; KQ474091; KPV71838.1; -; Genomic_DNA.
DR   RefSeq; XP_018267887.1; XM_018412920.1.
DR   AlphaFoldDB; A0A0P9F840; -.
DR   STRING; 578459.A0A0P9F840; -.
DR   GeneID; 28973369; -.
DR   OMA; DGPPCCY; -.
DR   OrthoDB; 1420095at2759; -.
DR   Proteomes; UP000053890; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd00508; MopB_CT_Fdh-Nap-like; 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; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053890}.
FT   DOMAIN          30..465
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          591..707
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   REGION          729..748
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        731..748
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   916 AA;  101182 MW;  1D15EADB1276CA6A CRC64;
     MKGRAVDRIN KGRLGPKGMY GWVSMKAEDR LKTPQIRNVE TGQLEPATWD EALSLMVEKA
     KGLVKEFTPH SIAFYTSGQL MLEEYHSLAL LGKAGFGTLH MDGNTRLCTA TAAAAMRESF
     GCDGQPGSYV DFDHCDTLFM VGHNMAATQT VLWSRILDRL AGPNPPFLIV ADPRRTSVGH
     AAVENGGIHL PARVGTNLCL LNGILKILLD SDEFHDSDFI SKHTIGIDAL RETVKDYPVE
     RVSEITGVDA ELIQQAAEKI GRSKRHVSTC LQGVYQSNQA TASACAVNNI HLVKGAIGKE
     GATVFQFNGQ PTAQNNRECG CNGEFPGFRN PSNPAHMQEL ADRWNIDVKT LPHYGQPTHI
     MSLLKFIENG SIKMLWISGT NPAVSMPELA RIRRNLASKD LFVVAQDIFP TETTALADVV
     LPAAQWAEKT GCGTNADRTV HLSHQAVKPP GEAWTDMKIF SEFSRRMDFK DKDGNPLIPW
     TDDAEAAFNH WKYTSKGRPV DYSGMSYEKL TGGSGVQWPC NDEHPDGCER LYTDFQFPTT
     LDTVESYGHD LFTGTVISPQ EFKALNPNGR AILKACHYHP QEEFVSDDYP FRLITGRVVH
     HFHTRTKTGR SKELEDAAPD VFVQISDADA AELGIESGDM ILVESARGSL EGPAKVGEIA
     RGDVFVPFHY GSADQDNEGG KKMRSRAANE LTLSAWDFVS KQPTFKGGAV RIKKVDGVQI
     HAVSGQYKAE QDRASAHKGE GLTEHKKEDH HRHLEDAIGE YDVFSKAVLD KMLELAKTHA
     DEMELRLGLK LHHKLCAQAS ERLQPVIDKY GEDATQAKTD VETIVKALFP RHRLGSKQFQ
     VMSDFTGFQT LLSHLIGWLH VLAPSLLALH DEESNKLVLA ASHLFEQARA WANDHNKVAA
     PQALIVPVVR HPDPPH
//
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