Reviewed, UniProtKB/Swiss-Prot P49050 (NIA_PICAN)

Names and origin

Protein names

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

Gene names

Name:

YNR1

Organism

Pichia angusta (Yeast) (Hansenula polymorpha)

Taxonomic identifier

4905 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Pichia

Protein attributes

Sequence length	859 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. 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
Technical term	3D-structure
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 – 859

859

Nitrate reductase [NADPH]

PRO_0000166044

Regions

Domain

502 – 578

77

Cytochrome b5 heme-binding

Domain

602 – 713

112

FAD-binding FR-type

Nucleotide binding

829 – 838

10

NADP By similarity

Sites

Metal binding

137

1

Molybdenum-pterin Potential

Metal binding

538

1

Iron (heme axial ligand) By similarity

Metal binding

561

1

Iron (heme axial ligand) By similarity

Amino acid modifications

Disulfide bond

383

Interchain Potential

Secondary structure

1

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859

Helix Strand Turn

Details...

Helix

38 – 41

4

Turn

44 – 47

4

Beta strand

54 – 58

5

Beta strand

63 – 65

3

Helix

69 – 74

6

Helix

81 – 83

3

Beta strand

86 – 90

5

Helix

97 – 102

6

Beta strand

104 – 113

10

Beta strand

115 – 118

4

Helix

119 – 125

7

Beta strand

129 – 136

8

Turn

138 – 141

4

Helix

142 – 148

7

Beta strand

161 – 170

10

Helix

171 – 178

8

Beta strand

186 – 192

7

Beta strand

201 – 205

5

Helix

206 – 209

4

Turn

212 – 214

3

Beta strand

217 – 222

6

Helix

229 – 231

3

Turn

232 – 234

3

Beta strand

236 – 238

3

Helix

244 – 246

3

Beta strand

249 – 259

11

Helix

264 – 267

4

Beta strand

268 – 271

4

Helix

279 – 284

6

Helix

286 – 289

4

Helix

292 – 294

3

Beta strand

302 – 308

7

Beta strand

313 – 315

3

Beta strand

320 – 328

9

Beta strand

335 – 343

9

Beta strand

352 – 354

3

Helix

357 – 362

6

Beta strand

365 – 368

4

Beta strand

371 – 373

3

Helix

375 – 377

3

Beta strand

385 – 392

8

Helix

393 – 397

5

Beta strand

400 – 408

9

Beta strand

431 – 438

8

Beta strand

441 – 445

5

Helix

456 – 462

7

Turn

470 – 473

4

Sequences

	Sequence		Length	Mass (Da)
	P49050-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 79569977B01E3967	FASTA	859	98,534
	10 20 30 40 50 60 MDSIVTEVTY GLEIKKIKDI TELPFPVRQD SPLTEVLPTD LKTKDNFVAR DPDLLRLTGS 70 80 90 100 110 120 HPFNSEPPLT KLYDSGFLTP VSLHFVRNHG PVPYVPDENI LDWEVSIEGM VETPYKIKLS 130 140 150 160 170 180 DIMEQFDIYS TPVTMVCAGN RRKEQNMVKK GAGFNWGAAG TSTSLWTGCM LGDVIGKARP 190 200 210 220 230 240 SKRARFVWME GADNPANGAY RTCIRLSWCM DPERCIMIAY QQNGEWLHPD HGKPLRVVIP 250 260 270 280 290 300 GVIGGRSVKW LKKLVVSDRP SENWYHYFDN RVLPTMVTPE MAKSDDRWWK DERYAIYDLN 310 320 330 340 350 360 LQTIICKPEN QQVIKISEDE YEIAGFGYNG GGVRIGRIEV SLDKGKSWKL ADIDYPEDRY 370 380 390 400 410 420 REAGYFRLFG GLVNVCDRMS CLCWCFWKLK VPLSELARSK DILIRGMDER MMVQPRTMYW 430 440 450 460 470 480 NVTSMLNNWW YRVAIIREGE SLRFEHPVVA NKPGGWMDRV KAEGGDILDN NWGEVDDTVK 490 500 510 520 530 540 QAERRPHIDE DLEMMCNREK MDVVIKYSEF EAHKDSETEP WFAVKGQVFD GSSYLEDHPG 550 560 570 580 590 600 GAQSILMVSG EDATDDFIAI HSSFAKKLLP SMHLGRLEEV SSVTKVKSVE QNVKREVLLD 610 620 630 640 650 660 PRKWHKITLA EKEVISSDSR IFKFDLEHSE QLSGLPTGKH LFLRLKDSSG KYVMRAYTPK 670 680 690 700 710 720 SSNSLRGRLE ILIKVYFPNR EYPNGGIMTN LIENLQVGNQ IEVKGPVGEF EYVKCGHCSF 730 740 750 760 770 780 NNKPYQMKHF VMISGGSGIT PTYQVLQAIF SDPEDRTSVQ LFFGNKKVDD ILLREELDHI 790 800 810 820 830 840 QEKYPEQFKV DYSLSDLDHL PENWSGVRGR LTFDILDTYV RGKKMGEYML LVCGPPGMNG 850 VVENWCNARK LDKQYVVYF

References

[1]	"Cloning and disruption of the YNR1 gene encoding the nitrate reductase apoenzyme of the yeast Hansenula polymorpha." Avila J., Perez M.D., Brito N., Gonzalez C., Siverio J.M. FEBS Lett. 366:137-142(1995) [PubMed: 7789531] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 14754 / IFO 0799 / JCM 3620 / NCYC 495 / NRRL Y-1798.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Z49110 Genomic DNA. Translation: CAA88925.1.

PIR

S65938.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BIH	X-ray	2.60	A	19-478	[»]
2BII	X-ray	1.70	A/B	59-478	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.7.1.3. 276392.

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_PICAN

Accession

Primary (citable) accession number: P49050

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
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)