ID   Q9URM3_PICAN            Unreviewed;      1044 AA.
AC   Q9URM3;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   07-APR-2021, entry version 89.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1 {ECO:0000256|ARBA:ARBA00018240};
GN   Name=YNI1 {ECO:0000313|EMBL:CAA11230.1};
OS   Pichia angusta (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=870730 {ECO:0000313|EMBL:CAA11230.1};
RN   [1] {ECO:0000313|EMBL:CAA11230.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=7789531; DOI=10.1016/0014-5793(95)00511-7;
RA   Avila J., Perez M.D., Brito N., Gonzalez C., Siverio J.M.;
RT   "Cloning and disruption of the YNR1 gene encoding the nitrate reductase
RT   apoenzyme of the yeast Hansenula polymorpha.";
RL   FEBS Lett. 366:137-142(1995).
RN   [2] {ECO:0000313|EMBL:CAA11230.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Brito N., Avila J., Perez M., Gonzalez C., Siverio J.;
RT   "The genes YNI1 and YNR1, encoding nitrite reductase and nitrate reductase
RT   respectively in the yeast Hansenula polymorpha, are clustered and
RT   coordinately regulated.";
RL   Biochem. J. 317:89-95(1996).
RN   [3] {ECO:0000313|EMBL:CAA11230.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=9020872;
RA   Perez M.D., Gonzalez C., Avila J., Brito N., Siverio J.M.;
RT   "The YNT1 gene encoding the nitrate transporter in the yeast Hansenula
RT   polymorpha is clustered with genes YNI1 and YNR1 encoding nitrite reductase
RT   and nitrate reductase, and its disruption causes inability to grow in
RT   nitrate.";
RL   Biochem. J. 321:397-403(1997).
RN   [4] {ECO:0000313|EMBL:CAA11230.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Avila J., Gonzalez C., Brito N., Siverio J.M.;
RT   "Clustering of the YNA1 gene encoding a Zn(II)2Cys6 transcriptional factor
RT   in the yeast Hansenula polymorpha with the nitrate assimilation genes YNT1,
RT   YNI1 and YNR1 and its involvment in their transcriptional activation.";
RL   Biochem. J. 335:647-652(1998).
RN   [5] {ECO:0000313|EMBL:CAA11230.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Avila J., Gonzalez C., Brito N., Machin F., Perez M., Siverio J.;
RT   "A second Zn(II)cCys6 transcriptional factor encoded by the YNA2 gene is
RT   indispensable for nitrate induction of the genes involved in nitrate
RT   assimilation in the yeast Hansenula polymorpha.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:CAA11230.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Siverio J.M.;
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC         Evidence={ECO:0000256|ARBA:ARBA00001929};
CC   -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC       {ECO:0000256|ARBA:ARBA00005096}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. PYROXD1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008147}.
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC       family. {ECO:0000256|ARBA:ARBA00010429}.
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DR   EMBL; AJ223294; CAA11230.1; -; Genomic_DNA.
DR   PIR; T43155; T43155.
DR   UniPathway; UPA00653; -.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:InterPro.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway.
DR   CDD; cd03529; Rieske_NirD; 1.
DR   Gene3D; 1.10.10.1100; -; 1.
DR   Gene3D; 2.102.10.10; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR   InterPro; IPR012744; Nitri_red_NirB.
DR   InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR   InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR   InterPro; IPR012748; Rieske-like_NirD.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR041575; Rubredoxin_C.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF13806; Rieske_2; 1.
DR   Pfam; PF18267; Rubredoxin_C; 1.
DR   PRINTS; PR00397; SIROHAEM.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55124; SSF55124; 1.
DR   TIGRFAMs; TIGR02378; nirD_assim_sml; 1.
DR   TIGRFAMs; TIGR02374; nitri_red_nirB; 1.
DR   PROSITE; PS00365; NIR_SIR; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:CAA11230.1}.
FT   DOMAIN          892..997
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   1044 AA;  116642 MW;  F946D5C52889EB4F CRC64;
     MTCSVPPLPE DISPRAAKKK LVIVGLGMVG LSFLEKLLSN DSKLNEYSIM VYGEEPYLAY
     NRVGLTEYFQ HREFKNLLLS PEEFYQLRGE KWNYAIDEKV VDIDRRARII TTDKGNRASY
     DVLVLCTGSA AILPTDLLPP LTRKSYREMG CFVYRTIDDL YSMIDYCQGA KKTRAIVVGG
     GLLGLEAAKA LYDMESFEDI TIVHRSHWLL SQQMDQKGGS LLTSKVKELG ITCRTGTTVS
     ELLFDEDQNL KGVKYDNGQI EECSLLCYTI GIKPRDELTS CGLNAGSRGG FKVNNMLQTS
     DENIYAIGEC ASWNNMTFGL IAPGYEMADI LAFNLTQGKL HQPKEFSEPS MGTRLKLMGV
     DVASFGDFFA DRNGPKWLLA DTTKKFVDLV FEDPIDATYT KLLFTKDGKY MLGGILVGDT
     SNYTKFSAMI RKPLPKSPSE LLIGKSGEDD MEMLSDETQI CSCHNITKGK LVEAVKNGCS
     SLADVKKCTK AGTACGGCEP TVKIIFEKEL KKLGGKVSNN LCVHFDYSRA HWFSLIMVKN
     FRSFRRVMEE LGNDPSSSGC EICKPTIGSI LSTLYNRHLL KKEVHGLQDT NDRYLGNIQR
     DGTFSVVPRM SAGEITPEKL VSIGKIAKKY GVYTKITGAQ RLDLFGVKKS DLLKIWKDLN
     EAGFESGQAY GKSLRNVKSC VGSTWCRYGI GDSVGLAVRL EERYKGIRSP HKMKGGVSGC
     VRDCAEFHSK DFGLCAVSGG FNIYVGGNGG MKPRHAQLLA TNVRPDEVIP ILDRYLMFYI
     TTADRLQRTA RWLENLDGGI EYLKDVIIRD KLGICKDLEA QMRHVVAGYY DEWAKAVSEE
     KENPIFKQFV NTPENQDCVE IVNERGQPRP AMWPEKAANQ KFNEIRWSSV SWQEVCECSD
     LPLAEAGSSA TVLVGDTQIA LFRTSKNELY CSQNMCGHKR AFVLNQGLLS EDSDKNCYIS
     CPMHKRNFYL KSGACKNDEA LSIATFEVKE ENGKVYAKLP PLKELDEVLG TSKWKVTSQE
     TEAKQVRKIT TEKNLVDKAI LLDW
//