ID A0A1L9Q349_ASPVE Unreviewed; 871 AA.
AC A0A1L9Q349;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=4Fe-4S Mo/W bis-MGD-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASPVEDRAFT_47378 {ECO:0000313|EMBL:OJJ08195.1};
OS Aspergillus versicolor CBS 583.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1036611 {ECO:0000313|EMBL:OJJ08195.1, ECO:0000313|Proteomes:UP000184073};
RN [1] {ECO:0000313|Proteomes:UP000184073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 583.65 {ECO:0000313|Proteomes:UP000184073};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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; KV878139; OJJ08195.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9Q349; -.
DR STRING; 1036611.A0A1L9Q349; -.
DR VEuPathDB; FungiDB:ASPVEDRAFT_47378; -.
DR OrthoDB; 1420095at2759; -.
DR Proteomes; UP000184073; 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 GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR CDD; cd02791; MopB_CT_Nitrate-R-NapA-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; IPR041957; CT_Nitrate-R-NapA-like.
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 Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000184073}.
FT DOMAIN 3..408
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 533..644
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 871 AA; 97597 MW; FC7021F2591CA90D CRC64;
MSLIVDRAKD IQSRLTNHGI GFYTSGQLML EEYYVLAMVG KAGLNTLHMD GNTRLCTATA
AASMRESFGS DGQPGSYADI DYTDCLFLVG HNMAATQTVL WSRVLDRLAG PNPPVLIVVD
PRMSDTAKKA TIHLSPKIGT NVALMNGLQH LIIENGWVNE DYTAKHVCGI DDLKKTVKEY
RPEYVERITG VPVSQLHETA RALATSGSLL STALQGVYQS NQATAAACQI NNINLLLGHI
GKPGSGILQM NGQPTAQNNR ETGCDGEYPG FRNHQNPQHM QEIADIWNID LTHVPHWNEP
THIQNMLNFI AAGSIEMFWV SGTNPLVSLP HLYRVRDLLT KPDLFLVVQD IFLTETAAIA
DVVLPAAQWG EKTGCFTNVD RTMHLSQKAV EPPGEAKPDL EIFLDFARRM DFCNKDGGVL
IPFTKPEEVF AEWKRMSSGR PLDCSALSYE KLTGGSGIQW PCTKEYPYGK ERLFEDGIFF
TDTEYCESFG HDLDTGAPLT KAQYQAMNPA GRAIFKSCHY KPSLEQPDNE FPFLLATGRN
VFHFHTRTKT GRSKRLQGAD RDACVVVSQT DADNIGVSNG EMVIVRSRRG QVELPVKTEG
INTGHVFIPF HFGYFDSKDK RARAANELTI EQWDPVSKQP TFKSGAVRIE KCVQKESQPP
IAPERQTAAI HAVKENKTNA KETGNRNDKS QNRIRWLEMW LGATHESLEM LRDIYSDLIP
RLVHDLEIQS GLEVMRRITY DAIERLEPVI SRYHESRRYG RKVCERLRRS LFPMEEDVSN
DVYEALIALQ SLEMFLTYIE GHLTALTPAS QALWDTEFVN AVTFAQTSVG RQKAWVTQHI
KVKSPQTLLV PQKPLSQLDT SASGLAREFY Y
//
