NIR_EMENI
ID NIR_EMENI Reviewed; 1104 AA.
AC P22944; C8VU59; Q5BEM3;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Nitrite reductase [NAD(P)H];
DE EC=1.7.1.4;
GN Name=niiA; ORFNames=AN1007;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX 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., Brow M.A.D.,
RA 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 A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., 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).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
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.
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000305}.
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DR EMBL; M58289; AAA33315.1; -; Genomic_DNA.
DR EMBL; AACD01000015; EAA65575.1; -; Genomic_DNA.
DR EMBL; BN001308; CBF88349.1; -; Genomic_DNA.
DR PIR; JH0181; JH0181.
DR RefSeq; XP_658611.1; XM_653519.1.
DR AlphaFoldDB; P22944; -.
DR SMR; P22944; -.
DR STRING; 162425.CADANIAP00001642; -.
DR PRIDE; P22944; -.
DR EnsemblFungi; CBF88349; CBF88349; ANIA_01007.
DR EnsemblFungi; EAA65575; EAA65575; AN1007.2.
DR GeneID; 2876784; -.
DR KEGG; ani:AN1007.2; -.
DR VEuPathDB; FungiDB:AN1007; -.
DR eggNOG; KOG1336; Eukaryota.
DR HOGENOM; CLU_003291_0_0_1; -.
DR InParanoid; P22944; -.
DR OMA; FAQVDPW; -.
DR OrthoDB; 528118at2759; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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:0020037; F:heme binding; IEA:InterPro.
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 GO; GO:0006807; P:nitrogen compound metabolic process; IMP:AspGD.
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; 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; PF13806; Rieske_2; 1.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF50022; SSF50022; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
DR SUPFAM; SSF55124; SSF55124; 1.
DR SUPFAM; SSF56014; SSF56014; 1.
DR TIGRFAMs; TIGR02378; nirD_assim_sml; 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; Metal-binding;
KW NADP; Nitrate assimilation; Oxidoreductase; Reference proteome.
FT CHAIN 1..1104
FT /note="Nitrite reductase [NAD(P)H]"
FT /id="PRO_0000199958"
FT DOMAIN 932..1040
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT REGION 396..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44..79
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 146..176
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 720
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 726
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 760
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 764
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 764
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 976
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 978
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 1001
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 1004
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT CONFLICT 709
FT /note="A -> R (in Ref. 1; AAA33315)"
FT /evidence="ECO:0000305"
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
