Reviewed, UniProtKB/Swiss-Prot P27969 (NIA2_HORVU)

Names and origin

Protein names	Recommended name:     Nitrate reductase [NADH]       Short name=NR     EC=1.7.1.1
Organism	Hordeum vulgare (Barley)
Taxonomic identifier	4513 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum

Protein attributes

Sequence length	912 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
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.
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 – 912	›912	Nitrate reductase [NADH]		PRO_0000166057
Regions
	Domain	535 – 610	76	Cytochrome b5 heme-binding
	Domain	651 – 764	114	FAD-binding FR-type
Sites
	Metal binding	186	1	Molybdenum-pterin Potential
	Metal binding	240	1	Molybdenum-pterin Potential
	Metal binding	570	1	Iron (heme axial ligand) By similarity
	Metal binding	593	1	Iron (heme axial ligand) By similarity
Amino acid modifications
	Disulfide bond	425		Interchain Potential
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P27969-1 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 47AB9C5B303190CC	FASTA	912	101,467
	10 20 30 40 50 60 SVEPRQPFGR LDAPATAPTA RAPGSNGIRR RADSPVRGCG FPSLISPPRK GPVAEEDEED 70 80 90 100 110 120 DDEDDEGHED WREAYGSHLQ LEVEPSTRDP RDEGTADAWI ERNPSLIRLT GKHPLNCEPP 130 140 150 160 170 180 LARLMHHGFI TPAPLHYVRN HGAVPRGDWA TWTVEVTGLV RRPARLTMDE LANGFPAAEV 190 200 210 220 230 240 PATLVCAGNR RKEQNMVQQT VGFNWGAAGV STSVWRGARL RDVLLRCGVM SKKGQALNVC 250 260 270 280 290 300 FEGAEDLPGG GGSKYGTSMS REWAMDPSRD IILPYAQNGE PLLPDHGYPV RVLIPGCIGG 310 320 330 340 350 360 RMVKWVRRIV VTTAESDNYY HFKDNRVLPS HVDAELANAE AWWYRPEYII NELNTNSVIT 370 380 390 400 410 420 TPGHDEILPI NAFTTQRAYT IKGYAYSGGG KKITRVEVTL DGGESWMLCT LDIPEKPNKY 430 440 450 460 470 480 GRYWCWCFWS VEIEVLDLLG AKEVAVRAWD QTHNTQPEKL IWNLMGMMNN CWFKIKVNVC 490 500 510 520 530 540 RPHKGEIGLV FEHPTQPGNQ TGGWMARQKH LETAEAAAPG LKRSTSTPFM NTAGDKQFTM 550 560 570 580 590 600 SEVRKHGSKE SAWIVVHGHV YDCTAFLKDH PGGADSILIN AGSDCTEEFD AIHSDKAKAL 610 620 630 640 650 660 LDTYRIGELI TTGTGYNSDN SVHGGSSLSH LAPIREATKV AGAPIALSSP REKVPCRLVD 670 680 690 700 710 720 KKELSHDVRL FRFALPSSDQ VLGLPVGKHI FVCATIDGKL CMRAYTPTSM VDEIGQFELL 730 740 750 760 770 780 VKVYFRDEHP KFPNGGLMTQ YLESLQVGSS SIDVKGPLGH VEYTGRGNFV INGKQRRARR 790 800 810 820 830 840 LAMICGSSGI TPMYQVIQAV LRDQPEDETE MHLVYANRSE DDILLRDELD RWATEYPDRL 850 860 870 880 890 900 KVWYVIDQVK RPEDGWKFSV GFVTEDILRA HVPEGGDDTL ALACGPPPMI KFAISPNLEK 910 MKYDMANSFI SF

References

[1]	"Analysis of barley nitrate reductase cDNA and genomic clones." Schnorr K.M., Juricek M., Huang C., Culley D., Kleinhofs A. Mol. Gen. Genet. 227:411-416(1991) [PubMed: 1865878] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Steptoe. Tissue: Leaf.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X57844 mRNA. Translation: CAA40975.1.
PIR	RDBHNS. S17454.
3D structure databases
HSSP	HSSP built from PDB template 2CND based on UniProtKB P17571.
SMR	P27969. Positions 653-912.
ModBase	Search...
Organism-specific databases
Gramene	P27969.
Enzyme and pathway databases
BRENDA	1.7.1.1. 283.
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

NIA2_HORVU

Accession

Primary (citable) accession number: P27969

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	June 16, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)