P36858 (NIA_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:

niaD

Organism

Aspergillus niger

Taxonomic identifier

5061 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	867 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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. Binds 1 heme group. The heme group is called cytochrome b-557. Binds 1 molybdenum ion.
Subunit structure	Homodimer By similarity.
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
Gene Ontology (GO)
Biological process	nitrate assimilation Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro molybdenum ion binding Inferred from electronic annotation. Source: InterPro 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 – 867	867	Nitrate reductase [NADPH]		PRO_0000166040
Regions
	Domain	514 – 589	76	Cytochrome b5 heme-binding
	Domain	615 – 726	112	FAD-binding FR-type
	Nucleotide binding	837 – 846	10	NADP By similarity
Sites
	Metal binding	152	1	Molybdenum-pterin Potential
	Metal binding	203	1	Molybdenum-pterin Potential
	Metal binding	549	1	Iron (heme axial ligand) By similarity
	Metal binding	572	1	Iron (heme axial ligand) By similarity
Amino acid modifications
	Disulfide bond	399		Interchain Potential

Sequences

	Sequence		Length	Mass (Da)
	P36858 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: BE40335DCBE12E42	FASTA	867	97,189
	10 20 30 40 50 60 MATVTEVLTE PFTAQGVTLK SGPIKVHQEE LPAVELSDIP LPPPSKEPTE VLSIDKPTPD 70 80 90 100 110 120 YHVPRDPRLI RLTGVHPFNV EPPLTALYDE GFLTSPELFY VRNHGPVPLV KDEDIPNWEI 130 140 150 160 170 180 SIEGLVEKPL VLNFRDILQQ YDQITAPITL VCAGNRRKEQ NVVRKTKGFS WGSAGLSTAL 190 200 210 220 230 240 WTGPMMADIL RSAKPLRKAK YVCMEGADKL PNGYYGTSIK LNWAMDPNRG IMLAHKMNGE 250 260 270 280 290 300 DLRPDHGRPL RAVVPGQIGG RSVKWLKKLI LTDAPSDNWY HIYDNRVLPT MVSPEMSSSD 310 320 330 340 350 360 PNWWRDDRYA IYDLNVNSSV VYPEHKEVLD LASAGPSYNV KGYAYAGGGR RITRVEISLD 370 380 390 400 410 420 KGKSWRLANI SYAEDKYRDF EGDLFGGRVH MSWRETCFCW CFWSLDIAIP ELENTDAILV 430 440 450 460 470 480 RAMDEALALQ PRDMYWSVLG MMNNPWFRVT ITKENGTLRF EHPTDPTGPG GWMERVKKAG 490 500 510 520 530 540 GDLVNGYWGE RQAGEEPTEP EPEKEINMKK EGVNRIIDLQ EFKKNSSDEK PWFIVNGEVY 550 560 570 580 590 600 DGTAFLEGHP GGAQSIISSA GIDVSEEFLA IHTQTAKAMM PDYHIGTMDK ASLEALKNDN 610 620 630 640 650 660 APQSDEPRAT FLQSKSWTKA TLVKRTDVSW DTRIFTFQLQ HDKQTLGLPI GQHLMIKVAD 670 680 690 700 710 720 PTSKEAIIRS YTPISDTNQE GTMDLLVKIY FDTPTVKGGK MTMALEKLAL GSEIDCKGPT 730 740 750 760 770 780 GRFEYLGNGK ILVSGKERHV SSFKMICGGT GITPIFQVLR AVMQDKQDPT SCVVLDGNRQ 790 800 810 820 830 840 EEDILCRADL DAYEALDSKK CKVVHTLTKA PDSWTGRRGR ISEDLLKEHA IPDGKSMVLI 850 860 CGPEAMEKSA RKILLEQGWA ESDLHFF

References

[1]	"The Aspergillus niger niaD gene encoding nitrate reductase: upstream nucleotide and amino acid sequence comparisons." Unkles S.E., Campbell E.I., Punt P.J., Hawker K.L., Contreras R., Hawkins A.R., van den Hondel C.A.M.J.J., Kinghorn J.R. Gene 111:149-155(1992) [PubMed: 1541396] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M77022 Genomic DNA. No translation available.
PIR	JQ1525.
3D structure databases
ProteinModelPortal	P36858.
SMR	P36858. Positions 40-491.
ModBase	Search...
Protein-protein interaction databases
STRING	P36858.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR001199. Cyt_B5. IPR018506. Cyt_B5_heme-BS. IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR014756. Ig_E-set. IPR005066. MoCF_OxRdtse_dimer. IPR008335. Mopterin_OxRdtase_euk. IPR001834. NADH-Cyt_B5_reductase. IPR012137. Nitr_rd_NADH. IPR008333. OxRdtase_FAD-bd_dom. IPR001433. OxRdtase_FAD/NAD-bd. IPR000572. OxRdtase_Mopterin-bd_dom. IPR022407. OxRdtase_Mopterin_BS. IPR017938. Riboflavin_synthase-like_b-brl. [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]
PIRSF	PIRSF000233. Nitr_rd_NADH. 1 hit.
PRINTS	PR00406. CYTB5RDTASE. PR00363. CYTOCHROMEB5. PR00407. EUMOPTERIN. PR00371. FPNCR.
SUPFAM	SSF55856. Cyt_B5. 1 hit. SSF81296. Ig_E-set. 1 hit. SSF56524. Oxidored_molyb. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
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_ASPNG

Accession

Primary (citable) accession number: P36858

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	September 21, 2011
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program