ID A0A2W1HPU8_9PLEO Unreviewed; 1157 AA.
AC A0A2W1HPU8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Nitrite reductase {ECO:0000313|EMBL:PWO19093.1};
GN ORFNames=Ptr86124_010777 {ECO:0000313|EMBL:KAI1510331.1}, PtrM4_01985
GN {ECO:0000313|EMBL:PWO19093.1}, PtrM4_119680
GN {ECO:0000313|EMBL:KAF7569553.1};
OS Pyrenophora tritici-repentis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=45151 {ECO:0000313|EMBL:PWO19093.1};
RN [1] {ECO:0000313|EMBL:PWO19093.1, ECO:0000313|Proteomes:UP000245464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M4 {ECO:0000313|EMBL:PWO19093.1,
RC ECO:0000313|Proteomes:UP000245464};
RX PubMed=29685100; DOI=10.1186/s12864-018-4680-3;
RA Moolhuijzen P., See P.T., Hane J.K., Shi G., Liu Z., Oliver R.P.,
RA Moffat C.S.;
RT "Comparative genomics of the wheat fungal pathogen Pyrenophora tritici-
RT repentis reveals chromosomal variations and genome plasticity.";
RL BMC Genomics 19:279-279(2018).
RN [2] {ECO:0000313|EMBL:KAI1510331.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=86-124 {ECO:0000313|EMBL:KAI1510331.1};
RA Moolhuijzen P.M., Moffat C.S.;
RL Submitted (MAY-2021) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAI1510331.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=86-124 {ECO:0000313|EMBL:KAI1510331.1};
RA Moolhuijzen P., See P.T., Shi G., Powell H.R., Cockram J., Jorgensen L.N.,
RA Benslimane H., Strelkov S.E., Turner J., Liu Z., Moffat C.S.;
RT "A global pangenome for the wheat fungal pathogen Pyrenophora tritici-
RT repentis and prediction of effector protein structural homology.";
RL bioRxiv 0:0-0(2022).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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 nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000256|ARBA:ARBA00010429}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWO19093.1}.
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DR EMBL; NQIK02000006; KAF7569553.1; -; Genomic_DNA.
DR EMBL; NRDI02000017; KAI1510331.1; -; Genomic_DNA.
DR EMBL; NQIK01000001; PWO19093.1; -; Genomic_DNA.
DR OMA; MWGGVTN; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000245464; Unassembled WGS sequence.
DR Proteomes; UP000249757; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster 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: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; 3.90.480.20; -; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 1.
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; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
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 NCBIfam; TIGR02378; nirD_assim_sml; 1.
DR PANTHER; PTHR43809; NITRITE REDUCTASE (NADH) LARGE SUBUNIT; 1.
DR PANTHER; PTHR43809:SF1; NITRITE REDUCTASE (NADH) LARGE SUBUNIT; 1.
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; PF00355; Rieske; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF50022; ISP domain; 1.
DR SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 1.
DR SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 1.
DR PROSITE; PS00365; NIR_SIR; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 3: Inferred from homology;
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}.
FT DOMAIN 971..1079
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1157 AA; 127613 MW; 99ABEF87946EF25F CRC64;
MAETEPIVTE GIEPSSGESH SPPGERHITA TWGSKDGNIS NAQWNDAEAN KLPEKVADLE
RKGEIHDQHP RKRIVVVGLG MVGIAFIEKL LKYDVKRREY DIVVIGEEPH LAYNRVGLTS
FFQHRKVENL YLNPQEWYAS MPEGSLNYHL NTLVTEIDSV NKNVKTSSGQ TVSYDILVLA
TGSDALLPRH TPGHDAKGVF VYRTIEDLQR LIEFSSTRKG TTGTVVGGGL LGLEAAHAMM
DLEDFAKVKL IERNRWVLSR QLDGDAGGMV VEQVRALGLD VMLSKRVGKI VTTEDNFVKG
VVFEDGDEME CSCICFAIGI KSRDELARKA GIKCADRGGG IVVGGDLATS QPGIYAIGEC
ASWENQTFGL IAPGVEMADV LAFNLTQAKA HAPRKFKAPD LSTKLKLLGV EVASFGDFFA
DRDGPKNMPG RQRAEKKEAN GTSTRDRVKN LTDGPAPPPV KALTYKDPFQ QVYKKYLFTM
DGKYLLGGMM IGDTKDYIKL VPMVKNQKPL EMAPSELIVG AKKGDDDGSD LTDDTQICSC
HNVTKGDVVN ATKDGTCKSI GDVKSCTKAG TGCGGCMPLV QTIFNKTMAS MGNEVKNHLC
PHFEYSRADL FNIIYIKGLK NFASVMKEAG KDPNSLGCEA CKPTIGNIVS SLYNKHLLEL
NNRGLQDTND RFLANIQRNG TFSVVPRVSG GEITPEKLIV IGTVAKKYNL YTKITGGQRI
DMFGARKQDL PDIWQELIDG GMESGHAYAK SLRTVKSCVG TTWCRFGIGD SVGMAVRLEE
RYKSIRGPHK IKGGVSGCVR ECAEAQNKDF GLIATEKGFN IFVGGNGGAK PRHSELLAKD
VPPDDVVPIL DRYLSFYIRT ADKLQRTARW MENLPGGIKY LQEVILEDKL GICADLEKQM
EDLVGTFFCE WTEVLKDPKK RSWFSQFANT SETIVDTIEP TEERGQQRPS YWPKDSITED
FRGTKWTELS WQPLVKADEF KDTDTGDSKA IKRGDTQLAV FKVRGKYYCT QQMCPHKRAF
VLSDGLIGDD IANNKLWVSC PYHKRNYELS GDNAGNCAND ESVNIAVFPI EERGDGWLYV
KLPSVEELDS VLGTSKFKIK KSETEDPFVA LDKKLQRMQL KGRKGMQVSH LEDGLGEKGR
AAQILAGGER GAGGLDW
//
