ID NIR_EMENI Reviewed; 1104 AA. AC P22944; Q5BEM3; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 2. DT 16-JUN-2009, entry version 71. DE RecName: Full=Nitrite reductase [NAD(P)H]; DE EC=1.7.1.4; GN Name=niiA; ORFNames=AN1007; OS Emericella nidulans (Aspergillus nidulans). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Emericella. OX NCBI_TaxID=162425; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=90382664; PubMed=2205530; DOI=10.1016/0378-1119(90)90178-T; RA Johnstone I.L., McCabe P.C., Greaves P., Gurr S.J., Cole G.E., RA Brow M.A.D., Unkles S.E., Clutterbuck A.J., Kinghorn J.R., Innis M.A.; RT "Isolation and characterisation of the crnA-niiA-niaD gene cluster for RT nitrate assimilation in Aspergillus nidulans."; RL Gene 90:181-192(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FGSC 4; RX PubMed=16372000; DOI=10.1038/nature04341; RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., RA Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., RA Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., RA Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C., RA Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., RA Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., RA Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., RA Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., RA Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.; RT "Sequencing of Aspergillus nidulans and comparative analysis with A. RT fumigatus and A. oryzae."; RL Nature 438:1105-1115(2005). CC -!- CATALYTIC ACTIVITY: Ammonium hydroxide + 3 NAD(P)(+) + H(2)O = CC nitrite + 3 NAD(P)H. CC -!- COFACTOR: Binds 1 siroheme per subunit. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity). CC -!- COFACTOR: FAD. CC -!- COFACTOR: Binds 1 2Fe-2S cluster per subunit (By similarity). CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation). CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S CC domain family. CC -!- SIMILARITY: Contains 1 Rieske domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M58289; AAA33315.1; -; Genomic_DNA. DR EMBL; AACD01000015; EAA65575.1; -; Genomic_DNA. DR PIR; JH0181; JH0181. DR HSSP; P37332; 1FQT. DR BRENDA; 1.7.1.4; 3859. 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:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0050660; F:FAD binding; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro. DR GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:EC. DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR ProDom; PD000139; FAD_pyr_redox; 1. DR PROSITE; PS00365; NIR_SIR; 1. DR PROSITE; PS51296; RIESKE; 1. PE 3: Inferred from homology; KW 2Fe-2S; 4Fe-4S; FAD; Flavoprotein; Heme; Iron; Iron-sulfur; KW Metal-binding; NADP; Nitrate assimilation; Oxidoreductase. FT CHAIN 1 1104 Nitrite reductase [NAD(P)H]. FT /FTId=PRO_0000199958. FT DOMAIN 932 1040 Rieske. FT NP_BIND 44 79 FAD (Potential). FT NP_BIND 146 176 NAD or NADP (Potential). FT METAL 720 720 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 726 726 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 760 760 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 764 764 Iron (siroheme axial ligand) (By FT similarity). FT METAL 764 764 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 976 976 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 978 978 Iron-sulfur (2Fe-2S); via pros nitrogen FT (By similarity). FT METAL 1001 1001 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 1004 1004 Iron-sulfur (2Fe-2S); via pros nitrogen FT (By similarity). FT CONFLICT 709 709 A -> R (in Ref. 1; AAA33315). SQ SEQUENCE 1104 AA; 122646 MW; 03CEA99309D7F691 CRC64; MPLLDGPRNG ETVTASAHNG IPIIDGVDPS TLRGDIDQDP NRRQKIVVVG LGMVAVAFIE KLVKLDSERR KYDIVVIGEE PHIAYNRVGL SSYFEHRKIE DLYLNPKEWY GSFKDRSFDY YLNTRVTDVF PQHKTVKTST GDIVSYDILV LATGSDAVLP TSTPGHDAKG IFVYRTISDL ERLMEFAANH KGQTGVTVGG GLLGLEAAKA MTDLEDFGSV KLIDRNKWVL ARQLDGDAGS LVTKKIRDLG LEVLHEKRVA KIHTDDDNNV TGILFEDGQE LDCCCICFAI GIRPRDELGG STGIQCAKRG GFVIDESLRT SVNDIYAIGE CASWENQTFG IIAPGIEMAD VLSFNLTNPD KEPKRFNRPD LSTKLKLLGV DVASFGDFFA DRDGPKFLPG QRPSAESIGA ADPNREEEPQ VKALTYRDPF GGVYKKYLFT MDGKYLLGGM MIGDTKDYVK LNQMVKSQKP LEVPPSEFIL GAQSGGEENA DDLDDSTQIC SCHNVTKGDV VESVKSGTCK TIADVKSCTK AGTGCGGCMP LVQSIFNKTM LDMGQEVSNN LCVHIPYSRA DLYNVIAIRQ LRTFDDVMKS AGKCPDSLGC EICKPAIASI LSSLFNPHLM DKEYHELQET NDRFLANIQR NGTFSVVPRV PGGEITADKL IAIGQVAKKY NLYCKITGGQ RIDMFGARKQ DLLDIWTELV DAGMESGHAY AKSLRTVKSC VGTTWCRFGV GDSVGMAIRL EQRYKSIRAP HKFKGAVSGC VRECAEAQNK DFGLIATEKG FNIFVGGNGG AKPRHSELLA KDVPPEEVIP ILDRYVIFYI RTADKLQRTA RWLESLPGGI EYLKDVVLND KLGIAAEMER QMQELVDSYF CEWTETVRNP KRRKYFQQFA NTDETVENVE IVKEREQVRP TYWPKDGANE DFKGHQWSSL SWQPVIKADY FSDGPPAISS ANIKRGDTQL AIFKVKGKYY ATQQMCPHKR TFVLSDGLIG DDDNGKYWVS CPYHKRNFEL NGEQAGRCQN DEAMNIATFP VEEREDGWIY MKLPPVEELD SVLGTEKWKV KKGEAVDPFE AYDKKYSGMK GKRAGAKGIE GSKPTRSPSN TIDW //