NIR_NEUCR
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 03-AUG-2022, entry version 151.
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=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;
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:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC 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; 5141.EFNCRP00000004474; -.
DR PRIDE; 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 BioCyc; MetaCyc:MON-12533; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
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: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 CDD; cd03529; Rieske_NirD; 1.
DR Gene3D; 1.10.10.1100; -; 1.
DR Gene3D; 2.102.10.10; -; 1.
DR Gene3D; 3.30.413.10; -; 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; 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 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; PR00397; SIROHAEM.
DR SUPFAM; SSF50022; SSF50022; 2.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55124; SSF55124; 1.
DR SUPFAM; SSF56014; SSF56014; 1.
DR TIGRFAMs; TIGR02374; nitri_red_nirB; 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 1005..1024
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1051
FT /note="Polar 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 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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 983
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 1058
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 1061
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
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
