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Database: UniProt
Entry: A0A0D1E0K7_USTMA
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ID   A0A0D1E0K7_USTMA        Unreviewed;      1372 AA.
AC   A0A0D1E0K7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=ferric-chelate reductase (NADPH) {ECO:0000256|ARBA:ARBA00012668};
DE            EC=1.16.1.9 {ECO:0000256|ARBA:ARBA00012668};
GN   ORFNames=UMAG_02730 {ECO:0000313|EMBL:KIS69396.1};
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS69396.1, ECO:0000313|Proteomes:UP000000561};
RN   [1] {ECO:0000313|EMBL:KIS69396.1, ECO:0000313|Proteomes:UP000000561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA   de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA   Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA   Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA   Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA   Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA   Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA   Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA   Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA   Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA   Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA   Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA   Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA   Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2] {ECO:0000313|Proteomes:UP000000561}
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-
CC         siderophore + NADPH; Xref=Rhea:RHEA:28795, Rhea:RHEA-COMP:11342,
CC         Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.16.1.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00000496};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC       {ECO:0000256|ARBA:ARBA00006278}.
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DR   EMBL; CM003145; KIS69396.1; -; Genomic_DNA.
DR   RefSeq; XP_011389096.1; XM_011390794.1.
DR   EnsemblFungi; KIS69396; KIS69396; UMAG_02730.
DR   GeneID; 23563406; -.
DR   KEGG; uma:UMAG_02730; -.
DR   VEuPathDB; FungiDB:UMAG_02730; -.
DR   eggNOG; ENOG502RDZM; Eukaryota.
DR   InParanoid; A0A0D1E0K7; -.
DR   OMA; WTKDLWD; -.
DR   OrthoDB; 1461913at2759; -.
DR   Proteomes; UP000000561; Chromosome 6.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0000293; F:ferric-chelate reductase activity; IBA:GO_Central.
DR   GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IBA:GO_Central.
DR   GO; GO:0033215; P:reductive iron assimilation; IBA:GO_Central.
DR   CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR013112; FAD-bd_8.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR013121; Fe_red_NAD-bd_6.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR   PANTHER; PTHR32361:SF28; FRP1P; 1.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   Pfam; PF08030; NAD_binding_6; 1.
DR   SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000561};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023065}.
FT   TRANSMEM        64..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        143..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        236..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        280..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        344..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          682..852
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          522..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          616..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          951..982
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1044..1064
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1084..1262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..450
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..507
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..570
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..636
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1044..1059
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1084..1099
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1106..1120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1184..1198
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1238..1255
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1372 AA;  151646 MW;  CD703B9A911ACB6D CRC64;
     MSSYSPGVSS SGGAYSPGVG SGSGSDSSSG CSGSCFDPNQ LKYQYLQGYF TAHMLPPSSY
     RYVYLLWFVT IVVCLVLGSF HMLGIGDRSY IGALWKRWAT KNRVYKLGKR VDIHGNFIQK
     DANGNSRAYA PLARRRIFTF PSFGRIVLLF FMLAVPIVLT LVGADYIGPN VGVFDFSQSW
     PSQTTNMAGL SRRAMHTLHK RVQWGQGNYP SVTTYPPYLT LPYHTWWTQG DRTGDITMGL
     VPIVLILALK QVPFALLSTR FFGGYAFDRL SFLHKWGGRI IWLFGTAHLV TWCIQLNKDT
     RIGEPVWSFV FMWTKFRWGW VSYGFLTAMI ILSIGPIRNR FYEWFYIAHV VTVAGFIITA
     MLHHPPLAQW MYIPLAWWVA ERLTRAFKVA WINGLGFAGR KPQFAIAPKP QTPYSHLSAG
     SDAPQRHVYR PYPSPYPSPS PSPSPSPSPS PQHQQLRNNY RDRSFGSRRQ YMDQTHGLGS
     HAPVTRPPTG SNRGPGTVAS SASSQKHVYM SRLSSEYEHT LIGSTSDNEP RKMSSPPIGV
     EAQGPLTTGA THPLDGRDDS SSESKHVALE RRATRVSARY DPVNDLIQDY IPSHMSNADV
     YPPQPTEALP PLPLQYAKQP STDTKHSLSD FAESQRPPTA PGSELVPMAS RRWQTESYAV
     SSTSPSNFSA RSNSVPRQLK PRPAMSADVA AVIRPGFAFV QLLPGKTLRL TLRTPNKMSW
     KPGQWVYLNV PSVRFWESHP FTIASAHDAD FPVATEFVDD DAEKGLAHTE KVKGEERTMV
     LLVRCRHGFT RHLWNFVAKK RQSQIQAAAD AQHGAYMYGI PGTSMVPILG KDTTGVHIRA
     IVDGPYGSAD RTHWGIHSTI VIVCGGSGVS FGMSVLEHLC ACMVGSMKFG KGGKGGKKFL
     TERVRFVWIM REFSHLQWVA AALRRCIEMV PPELLQVDLF VTHFNHLSAL PNGPRGRSAG
     ARSHHGGHKS ESDGPSYDTL AGGNGGAFLS EDAKYSRNAR FTEGPEQDEY DITAYDLTHF
     DGEDQSAPTA MEEEMNKRIR SEGKLRRAKT RRNTVKRKGG RGTKMADAEL NRDEQVLESQ
     RAMYEEHDDS LRQQPYEPER RPADGSWTSV QAQGALGSGN NGVLEQDLGD SGGRLLSSNS
     FVQPGWPPER RDRHAFGSNE RRHNSPPNSA GLLLPHGTMD SSVGPLSAYI SPSPSRPGSP
     HNELLPPPPF DSGSRASTPR LPPSPLTTPY GSEYPLRSDF RTPEDTEDSR RRGIMRGHAG
     SSTLNLLNTG VASAASPKSP LDDAPIDLDA EEDLDLRVVA ELAQPGHPKL DRIIRQEVEA
     SQGRTLVAGC GPKSLDIVLR SIVSKHIDAS KVRRGDTRGI VNVVSECFEW GG
//
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