NIR_LEPMC
ID NIR_LEPMC Reviewed; 185 AA.
AC P43504;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Nitrite reductase [NAD(P)H];
DE EC=1.7.1.4;
DE Flags: Fragment;
GN Name=NIIA;
OS Leptosphaeria maculans (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Leptosphaeria; Leptosphaeria maculans species complex.
OX NCBI_TaxID=5022;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate 19;
RX PubMed=7789806; DOI=10.1016/0378-1119(95)00169-7;
RA Williams R.S.B., Davis M.A., Howlett B.J.;
RT "The nitrate and nitrite reductase-encoding genes of Leptosphaeria maculans
RT are closely linked and transcribed in the same direction.";
RL Gene 158:153-154(1995).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O + 3 NADP(+) + NH4(+) = 5 H(+) + 3 NADPH + nitrite;
CC Xref=Rhea:RHEA:24632, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16301, ChEBI:CHEBI:28938, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.7.1.4;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O + 3 NAD(+) + NH4(+) = 5 H(+) + 3 NADH + nitrite;
CC Xref=Rhea:RHEA:24628, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16301, ChEBI:CHEBI:28938, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.7.1.4;
CC -!- COFACTOR:
CC Name=siroheme; Xref=ChEBI:CHEBI:60052; Evidence={ECO:0000250};
CC Note=Binds 1 siroheme per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR EMBL; U18793; AAA82739.1; -; Genomic_DNA.
DR PIR; PC4032; PC4032.
DR AlphaFoldDB; P43504; -.
DR SMR; P43504; -.
DR UniPathway; UPA00653; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106316; F:nitrite reductase NADH activity; IEA:RHEA.
DR GO; GO:0106314; F:nitrite reductase NADPH activity; IEA:RHEA.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; FAD; Flavoprotein; Heme; Iron; Iron-sulfur; Metal-binding; NADP;
KW Nitrate assimilation; Oxidoreductase.
FT CHAIN 1..>185
FT /note="Nitrite reductase [NAD(P)H]"
FT /id="PRO_0000199959"
FT REGION 14..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 72..107
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT NON_TER 185
SQ SEQUENCE 185 AA; 20756 MW; 19D67F97D386E7F9 CRC64;
MAATLPLLTQ GIEPVSGESY SPPGERHVQA TWGSKDGNIS NTEWNDPEAN RLPEKVAELE
KKGELNNSHP RRRVVVVGLG MVGVAFIEKL MKYDIKRREY DIIVIGEEPH LAYNRVGLTS
FFQHRQVENL YLNPQEWYSS MPEDSLHYHL NTLVTEIDSE NKTVKTSSGQ AVSYDILVLA
TGSSS