Reviewed, UniProtKB/Swiss-Prot P43101 (NIA_CICIN)

Names and origin

Protein names

Recommended name:
    Nitrate reductase [NADH]
      Short name=NR
    EC=1.7.1.1

Gene names

Name:

NIA

Organism

Cichorium intybus (Chicory)

Taxonomic identifier

13427 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › campanulids › Asterales › Asteraceae › Cichorioideae › Cichorieae › Cichorium

Protein attributes

Sequence length	920 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 + NAD+ + H2O = nitrate + NADH.
Cofactor	Binds 1 FAD per subunit. Binds 1 heme group per subunit. Binds 1 molybdenum-pterin group per subunit.
Subunit structure	Homodimer By similarity.
Tissue specificity	In cortical cells of roots grown at low nitrate concentrations, in vascular tissues of roots at high nitrate concentrations and in root apex under both conditions.
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 NAD
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 (NADH) 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 – 920	920	Nitrate reductase [NADH]		PRO_0000166054
Regions
	Domain	534 – 609	76	Cytochrome b5 heme-binding
	Domain	663 – 775	113	FAD-binding FR-type
Sites
	Metal binding	185	1	Molybdenum-pterin Potential
	Metal binding	239	1	Molybdenum-pterin Potential
	Metal binding	569	1	Iron (heme axial ligand) By similarity
	Metal binding	592	1	Iron (heme axial ligand) By similarity
Amino acid modifications
	Disulfide bond	424		Interchain Potential

Sequences

	Sequence		Length	Mass (Da)
	P43101-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: FE1E332CCC9A4D58	FASTA	920	103,520
	10 20 30 40 50 60 MAASVENRQF RHEPGLSAAG VVRSFSPNHR RSDSPIRNCN YPAAAREFMT PKKLPPETYD 70 80 90 100 110 120 TSDDEEDEAD YRDAIKKSNS ELESSVFDPR DQGTADQWIE RNPSMVRLTG KHPFNSEPPL 130 140 150 160 170 180 NKLMQHGFIT PDPLHYVRNH GPVPNATWED WTVEICGLVK RPARFSMTQL VNEFPSREFP 190 200 210 220 230 240 VTLVCAGNRR KEQNLTKQTI GFNWGAAGIS TSVWKGVPLV HILKRCGIYS RKKGALNVCF 250 260 270 280 290 300 EGAEDLPGGG GSKYGTSIKI EMAMDPARDI ILAYMQNGEK LSPDHGFPVR MIIPGFIGGR 310 320 330 340 350 360 MVKWLKRIIV TTPESESYYH FKDNRVLPSH VDAELANSEG WWYKPEYIIN ELNINSVITT 370 380 390 400 410 420 PCHEEILPIN SWTTQRPYTL RGYAYSGGGK KVTRVEVTMD GGETWNVCTL DHKEKPTRYA 430 440 450 460 470 480 KYWCWCFWSL EVEVLDLLSA KEIAVRAWDE TLNTQPDKLI WNLMGMMNNC WFRVKTNMCK 490 500 510 520 530 540 PHKGEIGIVF EHPTQPGNQS GGWMAREKHL EISSELAHPT LKKSVSSPFM NTTSLTFTMS 550 560 570 580 590 600 EVKKHNSADS AWIVVHGHIY DCTSFLKDHP GGSDSILLNA GTDCTEEFDA IHSDKAKKLL 610 620 630 640 650 660 EEYRVGELIT MGYSSDSAAS SPNNSVHGAT NYLTLHLSLA TIKEIAPTRS VALIPKEIAP 670 680 690 700 710 720 TRREKIPCKL ISKTSVSHDV RLFRFALPSP DQVLGLPVGK HVFVCATIDD KLCMRAYTPT 730 740 750 760 770 780 STIDEVGYFE LLVKIYFKGV EPKFPNGGLM SQHLESMELG SSIEIKGPLG HIEYMGRGTF 790 800 810 820 830 840 SVHGKQKFAR KLAMFAGGTG ITPDLSSDAS YLKDPEDDTE MYVVYANRTE DDILLREELD 850 860 870 880 890 900 AWADKYSDRV KVWYVVAKSI REGWKYSEGF ITEDIMREHV PEVSEDTLAL ACGPPPMIQF 910 920 AINPNLEKMG YDIKNSLLVF

References

[1]

"Evidence for the nitrate-dependent spatial regulation of the nitrate reductase gene in chicory roots." Palms B., Goupil P., de Almeida Engler J., Van der Straeten D., Van Montagu M., Rambour S. Planta 200:20-27(1996) [PubMed: 8987617] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: cv. Witloof. Tissue: Leaf and Root.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X84103 Genomic DNA. Translation: CAA58909.1. X84102 mRNA. Translation: CAA58908.1.
PIR	S52301.
3D structure databases
SMR	P43101. Positions 84-511, 535-608, 665-920.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.7.1.1. 141254.
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. 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.
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_CICIN

Accession

Primary (citable) accession number: P43101

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 19, 2010
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)