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Database: UniProt
Entry: A0A061HDW5_BLUGR
LinkDB: A0A061HDW5_BLUGR
Original site: A0A061HDW5_BLUGR 
ID   A0A061HDW5_BLUGR        Unreviewed;      1352 AA.
AC   A0A061HDW5;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   28-JUN-2023, entry version 36.
DE   SubName: Full=Aldehyde oxidase {ECO:0000313|EMBL:EPQ62890.1};
DE   SubName: Full=Bgt-345 {ECO:0000313|EMBL:SUZ12417.1};
GN   ORFNames=BGT96224_345 {ECO:0000313|EMBL:EPQ62890.1},
GN   BGT96224V2_LOCUS5585 {ECO:0000313|EMBL:SUZ12417.1};
OS   Blumeria graminis f. sp. tritici 96224.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Blumeria.
OX   NCBI_TaxID=1268274 {ECO:0000313|EMBL:SUZ12417.1};
RN   [1] {ECO:0000313|Proteomes:UP000053110}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=96224 {ECO:0000313|Proteomes:UP000053110};
RX   PubMed=23852167; DOI=10.1038/ng.2704;
RA   Wicker T., Oberhaensli S., Parlange F., Buchmann J.P., Shatalina M.,
RA   Roffler S., Ben-David R., Dolezel J., Simkova H., Schulze-Lefert P.,
RA   Spanu P.D., Bruggmann R., Amselem J., Quesneville H.,
RA   Ver Loren van Themaat E., Paape T., Shimizu K.K., Keller B.;
RT   "The wheat powdery mildew genome shows the unique evolution of an obligate
RT   biotroph.";
RL   Nat. Genet. 45:1092-1096(2013).
RN   [2] {ECO:0000313|EMBL:EPQ62890.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=96224 {ECO:0000313|EMBL:EPQ62890.1};
RA   Oberhaensli S., Wicker T., Keller B.;
RT   "The wheat powdery mildew genome reveals unique evolution of an obligate
RT   biotroph.";
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SUZ12417.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=96224 {ECO:0000313|EMBL:SUZ12417.1};
RA   Quirk P.G., Krulwich T.A.;
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000127-2};
CC   -!- COFACTOR:
CC       Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000127-3};
CC       Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC       {ECO:0000256|PIRSR:PIRSR000127-3};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000127-3};
CC       Note=Binds 2 [2Fe-2S] clusters. {ECO:0000256|PIRSR:PIRSR000127-3};
CC   -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006849}.
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DR   EMBL; KE375145; EPQ62890.1; -; Genomic_DNA.
DR   EMBL; UIGY01000173; SUZ12417.1; -; Genomic_DNA.
DR   HOGENOM; CLU_001681_1_2_1; -.
DR   OrthoDB; 5485853at2759; -.
DR   Proteomes; UP000053110; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR   Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
DR   Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR002888; 2Fe-2S-bd.
DR   InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR   InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR   InterPro; IPR016208; Ald_Oxase/xanthine_DH.
DR   InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR   InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
DR   InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   InterPro; IPR022407; OxRdtase_Mopterin_BS.
DR   PANTHER; PTHR45444; XANTHINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR45444:SF3; XANTHINE DEHYDROGENASE; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 1.
DR   Pfam; PF03450; CO_deh_flav_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   Pfam; PF02738; MoCoBD_1; 1.
DR   Pfam; PF20256; MoCoBD_2; 1.
DR   PIRSF; PIRSF000127; Xanthine_DH; 1.
DR   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR   SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR   SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|PIRSR:PIRSR000127-3};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000127-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000127-3};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR000127-
KW   3};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000127-3};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505, ECO:0000256|PIRSR:PIRSR000127-
KW   3}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053110}.
FT   DOMAIN          13..99
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          242..426
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   ACT_SITE        1275
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-1"
FT   BINDING         51
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         56
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         59
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         81
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         120
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         123
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         155
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         157
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         350
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         373
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         435
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         774
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         805
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         809
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         887
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         919
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT   BINDING         921
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         1017
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT   BINDING         1086
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
SQ   SEQUENCE   1352 AA;  148683 MW;  750E65B381C5C2D2 CRC64;
     MPSLSSITDS WGGALRFYLN GTSIVLDRID PNTTLLEYIR DIGLTGTKLG CAEGGCGACT
     VVISQYNPTT HKIYHASVNA CLAPLISVDG KHVITIEGIG TTDRPHLTQE RIARGNGSQC
     GFCTPGIVMS LYALLRNNST PSAEDVEETF DGNLCRCTGY RPILDAAQTF SVGTKCCKLK
     TSDGCCMKAT NNTKIFEGLV IERDSSPSSS NRKPPQLIKY DHDTELIFPP ALTKHDFKPL
     VFGGHEKKWF RPVTVKQLLE IKNVCPSAKI VSGSTEHQIE LRFKAMQHAV SIYVGDIPEL
     KEFLFREDYV DIGGNVTLTD LETIALEAVD RYGPARAQVF SAIHKQLGYF AGRQIRNVGT
     PAGNLVTASP ISDLNPIFLA ANATIITKNI EGQKEIEMSQ FFNGYRRTAL PPNSIIFCIR
     IPILSEAGEF FQSYKHSKRK DDDIAIVNAA FKVTLSKSNV IKCANLVYGG MAPITIVAKN
     ASAYLNGKRI DDTTTIEGAM KSLEEDFNLS FSVPGGMATF RRSLAFGFFY RFYNEILSKL
     DFLNNYLDQE ETSEIKRKIS TGWEDKDCAI SYQQRIIGKP EPHLAALKQA CGEAQYTDDL
     FVRKNELFGS LVLSTKAHAK ILSVDYLPAL EIPGVVDWLD HTDMPSPKAN FWGAPISDET
     FFAVDEVFTA GQPIGIVLAS TPHSALQGSR AVKVKYNELP AILTIEEAIK NESYFQHSRY
     IKKGDTREAF SKADNIFTGF ARIGGQEHFY LETQACVAIP KPEDGEIEIY ASTQNPTETQ
     TYVAQVCNLS ANKVVCKVKR LGGGFGGKET RSVQLSAIVA LAAKKTGRPV RCQLNRDEDM
     ITSGQRHPFL AQWKVGVHKD GKIQALEAEV FCNAGWSQDL SAAVCDRALS HIDGCYSIPN
     IDVRGRLCKT NTMSNTAFRG FGGPQGLFIA ETFMEEIADR LDIPVETLRQ INLYKPGDST
     HFNQTLEDWH VPLMYQQVQD ESLYAERRKE VTKFNSLHRW KKRGLSLIPT KFGISFTALF
     LNQAGALVHV YQDGSILVAH GGTEMGQGLH TKMTMVAAEA LGVPLSAVFI SETATNTVAN
     TSSTAASASS DLNGYAILDA CTQINTRLVP YRAKLGPQAS MEELARAAYL DRVNLSANGF
     YKTPDIGYVW GENTGQMFFY FTQGVAMAEV EVDTLTGEWT CLRADVKMDV GKSINPSIDY
     GQVQGAFVQG MGLFTSEESL WYESGAMKGQ LATRGPGTYK IPGFRDIPQE FNVSLLKGVE
     WKNLRTIQRS RGVGEPPLFL GSAVFFAIRD SLKAARSQYG TSAEIGVDEG SGLLRLVSPA
     TTERIRTSCV DPIVERARVK ALEGERSFFV SI
//
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