ID   NIR_NEUCR               Reviewed;        1176 AA.
AC   P38681; Q7RVB5;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   02-SEP-2026, entry version 168.
DE   RecName: Full=Nitrite reductase [NAD(P)H];
DE            EC=1.7.1.4;
GN   Name=nit-6; ORFNames=NCU04720;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=8096840; DOI=10.1128/jb.175.8.2379-2392.1993;
RA   Exley G.E., Colandene J.D., Garrett R.H.;
RT   "Molecular cloning, characterization, and nucleotide sequence of nit-6, the
RT   structural gene for nitrite reductase in Neurospora crassa.";
RL   J. Bacteriol. 175:2379-2392(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NH4(+) + 3 NADP(+) + 2 H2O = nitrite + 3 NADPH + 5 H(+);
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=NH4(+) + 3 NAD(+) + 2 H2O = nitrite + 3 NADH + 5 H(+);
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;
CC       Note=Binds 1 siroheme per subunit.;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000250|UniProtKB:P05340, ECO:0000255|PROSITE-
CC         ProRule:PRU00628};
CC       Note=Binds 2 [2Fe-2S] clusters per subunit.
CC       {ECO:0000250|UniProtKB:P05340, ECO:0000255|PROSITE-ProRule:PRU00628};
CC   -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- INDUCTION: By nitrate.
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC       family. {ECO:0000305}.
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DR   EMBL; L07391; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CM002241; EAA31119.3; -; Genomic_DNA.
DR   PIR; A49848; A49848.
DR   RefSeq; XP_960355.3; XM_955262.3.
DR   AlphaFoldDB; P38681; -.
DR   SMR; P38681; -.
DR   STRING; 367110.P38681; -.
DR   PaxDb; 367110-P38681; -.
DR   EnsemblFungi; EAA31119; EAA31119; NCU04720.
DR   GeneID; 3876518; -.
DR   KEGG; ncr:NCU04720; -.
DR   VEuPathDB; FungiDB:NCU04720; -.
DR   HOGENOM; CLU_003291_0_0_1; -.
DR   InParanoid; P38681; -.
DR   OrthoDB; 432169at2759; -.
DR   BioCyc; MetaCyc:MONOMER-12533; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
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:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway.
DR   CDD; cd03529; Rieske_NirD; 1.
DR   FunFam; 3.30.413.10:FF:000007; Nitrite reductase [NAD(P)H] large subunit; 1.
DR   FunFam; 1.10.10.1100:FF:000002; Nitrite reductase large subunit; 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; IPR052034; NasD-like.
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; 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; TIGR02374; nitri_red_nirB; 1.
DR   NCBIfam; NF011565; PRK14989.1; 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; 1.
DR   SUPFAM; SSF50022; ISP domain; 2.
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   2: Evidence at transcript level;
KW   2Fe-2S; 4Fe-4S; FAD; Flavoprotein; Heme; Iron; Iron-sulfur; Metal-binding;
KW   NADP; Nitrate assimilation; Oxidoreductase; Reference proteome.
FT   CHAIN           1..1176
FT                   /note="Nitrite reductase [NAD(P)H]"
FT                   /id="PRO_0000199960"
FT   DOMAIN          942..1094
FT                   /note="Rieske; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          998..1051
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1124..1157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..23
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        998..1008
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1030..1049
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1124..1139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         26..60
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         183..215
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
FT   BINDING         496
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P05340"
FT   BINDING         498
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P05340"
FT   BINDING         531
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P05340"
FT   BINDING         534
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P05340"
FT   BINDING         717
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         723
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         757
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         761
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         761
FT                   /ligand="siroheme"
FT                   /ligand_id="ChEBI:CHEBI:60052"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         981
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         983
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         1058
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         1061
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   CONFLICT        357
FT                   /note="T -> S (in Ref. 1; L07391)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1176 AA;  127382 MW;  00CAA27C94D6A564 CRC64;
     MANTSLDMAS STSPSPSPES TTTPRKRIVV VGLGMVGIAF IEKLIKLDTQ RQYEIVVIGE
     EPHVAYNRVG LTSFFSHREV EQLYLNPLEW YKQHLQTSSL THHLSTAALS LSPATKSLTI
     SPPPSTPSLT TLPYDHLILA TGSSALLPTS TPGHDASGVF VYRNIADLQS LITWSSDTQI
     KGSTGVVVGG GLLGLEAAKA LMDLQVFGRV VVIERNGWVL SRQVDGEAGA LVLEGVRGLG
     VEVLTRKRVK EVECDESKDE GEKEKKRVKG IRFEDGEYLA CSTICFAIGI KARDELAREA
     GITCAERGGG GIVVDDSLQT SAPDVYAIGE CASWKGQTFG LIGPGVEMAD VLAFNFTQAH
     LHTPRVFKRP DLSTKLKLLG VEVASFGDFF ADRDGPKELP PKLRRELKKS GGKAEVKALT
     YKDPFLSVYK KYIFTSDGKY LLGGMMIGDT TDYVRLVPLV KTHKELDVPP SQLILGAKKS
     GDDNGDDDLP DDTQICSCHN VTKADLVAPL KSGECTSLGD LKSCTKAGTG CGGCMPLVTS
     IFNRTMASLG TEVKNNLCPH FPEYSRADLY NIISVKRLRT LPDVMREAGA DADSLGCEAC
     KPAIASIFAS LWNDHVMSPA HHGLQDTNDR FMGNIQRNGT FSVVPRVAAG EITPEKLIVI
     GEVAKEYNLY TKITGGQRID MFGAKKQDLL KIWKKLVDAG MESGHAYAKS LRTVKSCVGT
     TWCRYGVGDS VGMAVRLEER YKGLRGPHKI KGGVSGCTRE CAEAGNKDFG LIATEKGFNI
     LICGNGGTTP KHSVLLAKDV PPTNVIPIID RFLMFYIRTA DKLQRTARWL EALPGGIDYL
     KEVILEDRLG ICASLEAQMQ ELVDSYFDEW AEALNNPAMQ ERFKQFANTD EGQPPMEVEI
     DRGQERPVMW PREDEGGSAK ADFKGLRDKW SSTTWQPVLE ASYFQGADDL PNGISASIKR
     GDTQLAVWRI KGKYYASQQM CPHKRTFALS DGFVGTDPSP SSCSSSALPP SPPSTPPRSS
     SPVTSPPQSP TSSATPATTA SSSCTTNPSG PASPWISCPF HKRNFSLTSG SCKNDNELSI
     ATFDVEERDD GMVYIKLPPV DELDRELGTK KWMVKKGEAG EGQLRELDEL NKSKGVEGKK
     GRRGRKPGAS EAGKEVGKKL VEAVGGGGCG GPGLEW
//