Reviewed, UniProtKB/Swiss-Prot P08619 (NIA_NEUCR)

Names and origin

Protein names

Recommended name:
    Nitrate reductase [NADPH]
      Short name=NR
    EC=1.7.1.3

Gene names

Name:	nit-3
ORF Names:	NCU05298

Organism

Neurospora crassa [Complete proteome]

Taxonomic identifier

5141 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora

Protein attributes

Sequence length	982 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
Catalytic activity	Nitrite + NADP+ + H2O = nitrate + NADPH.
Cofactor	Binds 1 FAD per subunit. Binds 1 heme group per subunit. The heme group is called cytochrome b-557. Binds 1 molybdenum (molybdopterin) per subunit.
Pathway	Nitrogen metabolism; nitrate reduction (assimilation).
Subunit structure	Homodimer.
Induction	Its expression is highly regulated and responds rapidly to nitrate induction and to nitrogen repression.
Sequence similarities	Belongs to the nitrate reductase family. Contains 1 cytochrome b5 heme-binding domain. Contains 1 FAD-binding FR-type domain.

Ontologies

Keywords
Biological process	Nitrate assimilation
Ligand	FAD Flavoprotein Heme Iron Metal-binding Molybdenum NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	nitrate assimilation Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro molybdenum ion binding Inferred from electronic annotation. Source: UniProtKB-KW nitrate reductase (NADPH) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 982	982	Nitrate reductase [NADPH]		PRO_0000166046
Regions
	Domain	617 – 692	76	Cytochrome b5 heme-binding
	Domain	721 – 836	116	FAD-binding FR-type
	Nucleotide binding	952 – 961	10	NADP By similarity
Sites
	Metal binding	240	1	Molybdenum-pterin Potential
	Metal binding	295	1	Molybdenum-pterin Potential
	Metal binding	652	1	Iron (heme axial ligand) By similarity
	Metal binding	675	1	Iron (heme axial ligand) By similarity
Amino acid modifications
	Disulfide bond	499		Interchain Potential
Experimental info
	Mutagenesis	652	1	H → A: Little loss of enzyme activity.
	Mutagenesis	675	1	H → A: Loss of enzyme activity.
	Sequence conflict	31 – 49	19	VGCSS…LLVPH → AAAAAAEKNPRGAADYCPSD in EAA32833. Ref.2
	Sequence conflict	139	1	I → IP in EAA32833. Ref.2
	Sequence conflict	696	1	P → L in EAA32833. Ref.2
	Sequence conflict	869 – 870	2	AE → LR in EAA32833. Ref.2
	Sequence conflict	910	1	M → E in EAA32833. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P08619-1 [UniParc]. Last modified June 1, 1994. Version 3. Checksum: B7838C031B19687F	FASTA	982	108,433
	10 20 30 40 50 60 MEAPALEQRQ SLHDSSERQQ RFTSLILPNG VGCSSREEPQ GSGGLLVPHN DNDIDNDLAS 70 80 90 100 110 120 TRTASPTTTD FSSSSSDDNS TTLETSVNYS HSSNTNTNTS CPPSPITSSS LKPAYPLPPP 130 140 150 160 170 180 STRLTTILPT DLKTPDHLIR DPRLIRLTGS HPFNVEPPLT ALFEHGFLTP QNLHYVRNHG 190 200 210 220 230 240 PIPSSVATPP ATINKEEDDS LLNWEFTVEG LVEHPLKISV RELMDASKWD NVTYPVTLVC 250 260 270 280 290 300 AGNRRKEQNV LRKSKGFSWG AGGLSTALWT GVGLSEILAR AKPLTKKGGG ARYVCFEGAD 310 320 330 340 350 360 QLPNGTYGTS VKLAWAMDPN KGIMVAHKMN GENLHPDHGR PVRVVVPGQI GGRSVKWLKR 370 380 390 400 410 420 IVVTKGPSEN WYHVFDNRVL PTTVGPEESG EKTEEMERVW RDERYAIYDL NVNSVICEPG 430 440 450 460 470 480 HGEVVSLRGD EGAGTYRLRG YAYAGGGRRV TRLEVTLDQG KSWRLAGIEY PEDRYREAQD 490 500 510 520 530 540 GEELFGGRLD VSWRESCFCW CFWDLEIPLS ELRKAKDVCI RAMDESLALQ PKEMYWSVLG 550 560 570 580 590 600 MMNNPWFRVV IHHEGDTLRF EHPTQPMLTS DGWMDRVKKE GGNLANGFWG EKVPGAEENV 610 620 630 640 650 660 VKEEPVKEIS MVDEKVTRLI TLEELRQHDG EEEPWFVVNG QVYNGTPFLE GHPGGAASIT 670 680 690 700 710 720 GAAGQDVTDE FLAIHSENAK AMMPTYHIGT LTPSAPAALK SSSTSDPALS DPSRPIFLQS 730 740 750 760 770 780 KTWNSAILTF KESVSPDTKI FHFALSHPAQ SIGLPVGQHL MMRLPDPAKP TESIIRAYTP 790 800 810 820 830 840 ISDGTLERGT LRVLVKIYYA SPTEDIKGGQ MTQALDALAL GKAVEFKGPV GKFVYQGRGV 850 860 870 880 890 900 CSVNGRERKV KRFVMVCGGS GVTPIYQVAE AVAVDDQDGT ECLVLDGNRV EGDILMKSEL 910 920 930 940 950 960 DELVERAKPM GRCRVKYTLS RPGAEWEGLR GRLDKTMLER EVGEGDLRGE TMVLLCGPEG 970 980 MQNMVREVLK GMGWKDEDVL VF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nit-3, the structural gene of nitrate reductase in Neurospora crassa: nucleotide sequence and regulation of mRNA synthesis and turnover." Okamoto P.M., Fu Y.-H., Marzluf G.A. Mol. Gen. Genet. 227:213-223(1991) [PubMed: 1829499] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[2]	"The genome sequence of the filamentous fungus Neurospora crassa." Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W. Nature 422:859-868(2003) [PubMed: 12712197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[3]	"On the presence of a heme-binding domain homologous to cytochrome b5 in Neurospora crassa assimilatory nitrate reductase." Le K.H.D., Lederer F. EMBO J. 2:1909-1914(1983) [PubMed: 16453480] [Abstract] Cited for: PRELIMINARY PARTIAL PROTEIN SEQUENCE AROUND HIS-652.
[4]	"Molecular characterization of conventional and new repeat-induced mutants of nit-3, the structural gene that encodes nitrate reductase in Neurospora crassa." Okamoto P.M., Garrett R.H., Marzluf G.A. Mol. Gen. Genet. 238:81-90(1993) [PubMed: 8479443] [Abstract] Cited for: MUTANTS. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[5]	"Nitrate reductase of Neurospora crassa: the functional role of individual amino acids in the heme domain as examined by site-directed mutagenesis." Okamoto P.M., Marzluf G.A. Mol. Gen. Genet. 240:221-230(1993) [PubMed: 8355655] [Abstract] Cited for: MUTAGENESIS.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X61303 Genomic DNA. Translation: CAA43600.1. AABX02000019 Genomic DNA. Translation: EAA32833.1.
PIR	S16292.
3D structure databases
HSSP	HSSP built from PDB template 1M2M based on UniProtKB P00171.
ModBase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MON-13438.
BRENDA	1.7.1.3. 266.
Family and domain databases
InterPro	IPR001199. Cyt_B5. IPR018506. Cyt_B5_heme-BS. IPR017927. Fd_Rdtase_FAD-bd. IPR005066. MoCF_OxRdtse_dimer. IPR008335. Mopterin_OxRdtase_euk. IPR001834. NADH-Cyt_B5_reductase. IPR008333. OxRdtase_FAD-bd. IPR001433. OxRdtase_FAD/NAD_bd. IPR000572. OxRdtase_Mopterin-bd. [Graphical view]
Gene3D	G3DSA:3.10.120.10. Cyt_B5. 1 hit. G3DSA:2.60.40.650. MoCF_oxrdtse_dimer. 1 hit. G3DSA:3.90.420.10. Oxred_molyb_bd. 1 hit.
Pfam	PF00173. Cyt-b5. 1 hit. PF00970. FAD_binding_6. 1 hit. PF03404. Mo-co_dimer. 1 hit. PF00175. NAD_binding_1. 1 hit. PF00174. Oxidored_molyb. 1 hit. [Graphical view]
PRINTS	PR00406. CYTB5RDTASE. PR00363. CYTOCHROMEB5. PR00407. EUMOPTERIN.
ProDom	PD000612. Cyt_B5. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00191. CYTOCHROME_B5_1. 1 hit. PS50255. CYTOCHROME_B5_2. 1 hit. PS51384. FAD_FR. 1 hit. PS00559. MOLYBDOPTERIN_EUK. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NIA_NEUCR

Accession

Primary (citable) accession number: P08619
Secondary accession number(s): Q7RVF6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	June 1, 1994
Last modified:	June 16, 2009
This is version 93 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)