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Database: UniProt
Entry: G4V0Q2_NEUT9
LinkDB: G4V0Q2_NEUT9
Original site: G4V0Q2_NEUT9 
ID   G4V0Q2_NEUT9            Unreviewed;      1169 AA.
AC   G4V0Q2;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Nitrite reductase {ECO:0000313|EMBL:EGZ68542.1};
GN   ORFNames=NEUTE2DRAFT_118535 {ECO:0000313|EMBL:EGZ68542.1};
OS   Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ68542.1, ECO:0000313|Proteomes:UP000008513};
RN   [1] {ECO:0000313|EMBL:EGZ68542.1, ECO:0000313|Proteomes:UP000008513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX   PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to self-
RT   fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Genetics 189:55-69(2011).
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}.
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DR   EMBL; GL891269; EGZ68542.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4V0Q2; -.
DR   STRING; 510952.G4V0Q2; -.
DR   eggNOG; KOG1336; Eukaryota.
DR   HOGENOM; CLU_003291_0_0_1; -.
DR   OMA; MWGGVTN; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000008513; Unassembled WGS sequence.
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: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   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; 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; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   NCBIfam; TIGR02374; nitri_red_nirB; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008513}.
FT   DOMAIN          935..977
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
FT   REGION          991..1046
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1117..1150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        998..1013
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1014..1046
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1169 AA;  126807 MW;  FB3F66FB0EA405C4 CRC64;
     MASSTSPSPS PESTTPPRKR IVVVGLGMVG IAFIEKLIKL DTQRQYEIVV VGEEPHVAYN
     RVGLTSFFSH REVEQLYLNP LEWYKQHLQT SSLTHHLSTT ALSLSPATKS LTISPPPSTP
     SLTTLPYDHL ILATGSRALL PTSTPGHDAS GVFVYRTIAD LQSLITWSSD TQIKGSTGVV
     VGGGLLGLEA AKALMDLQVF GRVVVIERNG WVLSRQVDGE AGALVLEGVR GLGVEVLTRK
     RVKEVECDHG EDEGQKEKKR VKGIRFEDGE YLACSTICFA IGIKARDELA RQAGITCAER
     GGGGIVVDDS LQTSAADVYA IGECASWKGQ TFGLIGPGVE MADVLAFNFT QAHLHTPRVF
     KRPDLSTKLK LLGVEVASFG DFFADRDGPK ELPPKLRREL KKSGGKAEVK ALTYKDPFLS
     VYKKYIFTSD GKYLLGGMMI GDTTDYVRLV PLVKTHKELD IPPSQLILGA KKSGDDNGDD
     DLPDDTQICS CHNVTKADLV APLKSGECTS LGDLKSCTKA GTGCGGCMPL VTSIFNRTMA
     SLGTEVKNNL CPHFPEYSRA DLYNIISVKR LRTLPDVMRE AGADADSLGC EACKPAIASI
     FASLWNDHVM SPAHHGLQDT NDRFMGNIQR NGTFSVVPRV AAGEITPEKL IVIGEVAKEY
     NLYTKITGGQ RIDMFGARKQ DLLNIWKKLV DAGMESGHAY AKSLRTVKSC VGTTWCRYGV
     GDSVGMAVRL EERYKGLRGP HKIKGGVSGC TRECAEAGNK DFGLIATEKG FNILICGNGG
     TTPKHSVLLA KDVPPTNVIP IIDRFLMFYI RTADKLQRTA RWLEALPGGI DYLKEVILED
     RLGICASLEA QMQELVDSYF DEWAEALNNP AMQERFKQFA NTDEGQPPME VEIDRGQERP
     VMWPREDQGG SAKADFKGLR DKWSSTTWQP VLEASYFQGA DDLPNGISAS IKRGDTQLAV
     WRIKGKYYAS QQMCPHKRTF ALSDGFVGTD PSPSSCSSTA LPPSPPSTPP RSSSPVTSSP
     QSPTSSATPA TTTSSSCTTN PSGPSSPWIS CPFHKRNFSL TSGSCKNDNE LSIATFDVEE
     RDDGMVYIKL PPVDELDREL GTKKWMVKRG EAGEGQFREL DELNKSKGVE GKKGRRGRKP
     GASEAGKEVG KKLVEAVGGG GCGGPGLEW
//
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