Reviewed, UniProtKB/Swiss-Prot P22945 (NIA_EMENI)

Names and origin

Protein names

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

Gene names

Name:	niaD
ORF Names:	AN1006

Organism

Emericella nidulans (Aspergillus nidulans)

Taxonomic identifier

162425 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	873 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro 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 – 873	873	Nitrate reductase [NADPH]		PRO_0000166042
Regions
	Domain	512 – 587	76	Cytochrome b5 heme-binding
	Domain	616 – 729	114	FAD-binding FR-type
	Nucleotide binding	843 – 852	10	NADP By similarity
Sites
	Metal binding	150	1	Molybdenum-pterin Potential
	Metal binding	201	1	Molybdenum-pterin Potential
	Metal binding	547	1	Iron (heme axial ligand) By similarity
	Metal binding	570	1	Iron (heme axial ligand) By similarity
Amino acid modifications
	Disulfide bond	397		Interchain Potential

Sequences

	Sequence		Length	Mass (Da)
	P22945-1 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: BEE38281987A894C	FASTA	873	97,560
	10 20 30 40 50 60 MSTTVTQVRT GSIPKTLKTS QIRVEEQEIT ELDTADIPLP PPSKEPTEVL SLDKTTPDSH 70 80 90 100 110 120 VPRDPRLIRL TGVHPFNVEP PLTALFQQGF LTPPELFYVR NHGPVPHVRD EDIPNWELRI 130 140 150 160 170 180 EGLVEKPITL SFKQILQNYD QITAPITLVC AGNRRKEQNT VRKSKGFSWG SAALSTALFT 190 200 210 220 230 240 GPMMADIIKS AKPLRRAKYV CMEGADNLPN GNYGTSIKLN WAMDPNRGIM LAHKMNGEDL 250 260 270 280 290 300 RPDHGRPLRA VVPGQIGGRS VKWLKKLIIT DAPSDNWYHI YDNRVLPTMV TPDMSSQNPS 310 320 330 340 350 360 WWRDERYAIY DLNVNSAAVY PQHKETLDLA AARPFYTAKG YAYAGGGRRI TRVEISLDKG 370 380 390 400 410 420 KSWRLARIEY AEDKYRDFEG TLYGGRVDMA WREACFCWSF WSLDIPVSEL ASSDALLVRA 430 440 450 460 470 480 MDEALSLQPK DMYWSVLGMM NNPWFRVKIT NENGRLLFEH PTDITGSSGW MEQIKKAGGD 490 500 510 520 530 540 LTNGNWGERQ EGEEPVEAEP VVEVNMKKEG VTRIIDLEEF KKNSSDERPW FVVNGEVYDG 550 560 570 580 590 600 TAFLEGHPGG AQSIISAAGT DASEEFLEIH SETAKKMMPD YHIGTLDKAS LEALRKGNAD 610 620 630 640 650 660 TTDSSSDPRP TFLTPKAWTK ATLTKKTSVS SDTHIFTLSL EHPSQALGLP TGQHLMLKTP 670 680 690 700 710 720 DPKSSSSGSI IRSYTPISPS DQLGMVDILI KIYAETPSIP GGKMTTALDT LPLGSVIECK 730 740 750 760 770 780 GPTGRFEYLD RGRVLISGKE RFVKSFVMIC GGTGITPVFQ VLRAVMQDEQ DETKCVMLDG 790 800 810 820 830 840 NRLEEDILLK NELDEFEALA GKKEKCKIVH TLTKGSESWT GRRGRIDEEL IRQHAGTPDR 850 860 870 ETMVLVCGPE AMEKASKKIL LSLGWKEENL HYF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterisation of the crnA-niiA-niaD gene cluster for nitrate assimilation in Aspergillus nidulans." Johnstone I.L., McCabe P.C., Greaves P., Gurr S.J., Cole G.E., Brow M.A.D., Unkles S.E., Clutterbuck A.J., Kinghorn J.R., Innis M.A. Gene 90:181-192(1990) [PubMed: 2205530] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC 4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M58291 Genomic DNA. Translation: AAA33314.1. AACD01000015 Genomic DNA. Translation: EAA65574.1.
PIR	JH0182.
RefSeq	XP_658610.1.
3D structure databases
HSSP	HSSP built from PDB template 1ICC based on UniProtKB P04166.
ModBase	Search...
Genome annotation databases
GeneID	2876780.
KEGG	ani:AN1006.2.
Enzyme and pathway databases
BRENDA	1.7.1.3. 3859.
Family and domain databases
InterPro	IPR001199. Cyt_B5. IPR018506. Cyt_B5_heme-BS. IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR005066. MoCF_OxRdtse_dimer. IPR008335. Mopterin_OxRdtase_euk. IPR001834. NADH-Cyt_B5_reductase. IPR012137. Nitr_rd_NADH. 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]
PIRSF	PIRSF000233. Nitr_rd_NADH. 1 hit.
PRINTS	PR00406. CYTB5RDTASE. PR00363. CYTOCHROMEB5. PR00407. EUMOPTERIN. PR00371. FPNCR.
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_EMENI

Accession

Primary (citable) accession number: P22945
Secondary accession number(s): Q5BEM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	June 16, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)