Reviewed, UniProtKB/Swiss-Prot P39866 (NIA2_PHAVU)

Names and origin

Protein names

Recommended name:
    Nitrate reductase [NADH] 2
      Short name=NR-2
    EC=1.7.1.1

Gene names

Name:	NIA2
Synonyms:	NR2

Organism

Phaseolus vulgaris (Kidney bean) (French bean)

Taxonomic identifier

3885 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Phaseolus

Protein attributes

Sequence length	890 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 + NAD+ + H2O = nitrate + NADH.
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 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 – 890	890	Nitrate reductase [NADH] 2		PRO_0000166068
Regions
	Domain	513 – 588	76	Cytochrome b5 heme-binding
	Domain	634 – 746	113	FAD-binding FR-type
Sites
	Metal binding	165	1	Molybdenum-pterin Potential
	Metal binding	219	1	Molybdenum-pterin Potential
	Metal binding	548	1	Iron (heme axial ligand) By similarity
	Metal binding	571	1	Iron (heme axial ligand) By similarity
Amino acid modifications
	Disulfide bond	404		Interchain Potential

Sequences

	Sequence		Length	Mass (Da)
	P39866-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: FC03B96F0139DE1E	FASTA	890	99,995
	10 20 30 40 50 60 MAASVGNRQF ATHMNGVVRS CGQDLKPSLP LDFDLDSSSS DDDENDDASY LKELVRKANA 70 80 90 100 110 120 ETEASVMDPR DEGTADQWVA RNASMVRLTG KHPFNAESPL QRLMHHGFIT PVPLHYVRNH 130 140 150 160 170 180 GPVPKANWED WTVEITGLVK RPTRFTMDRL VREFPHREFP ATLVCAGNRR KEQNMVKKTI 190 200 210 220 230 240 GFNWGSAGTS TSVWRGVPVR HVLRRCGILT RGKGALHVSF EGAENLPGGG GSKYGTSISR 250 260 270 280 290 300 EMAMDPSRDI ILAYMQNGEP LAPDHGFPIR MIIPGFIGGR MVKWLKRIVV TEQECESHYH 310 320 330 340 350 360 YKDNRVLPSH VDPELANEEG WWFKPEYIIN ELNINSVITT PCHDEILPIN SWTTQRPYVV 370 380 390 400 410 420 RGYAYSGGGR KVTRVEVTLD GGETWHVCTL DHPEKPNKYG KYWCWCFWSL EVEVLDLLGT 430 440 450 460 470 480 KEIAVRAWDE GLNTQPENLI WNLMGMMNNC WFRVKTNVCK PHKGEIGIVF EHPTQPGNQP 490 500 510 520 530 540 GGWMAKEKHL EQSQEAKPSL KKSVSTPFMN TASKMFSVSE VKKHSSPDSA WIIVHGHVYD 550 560 570 580 590 600 CTRFLKDHPG GTDSILINAG TDCTEEFDAI HSDKAKKMLE DYRIGELITT GYTSADSSPN 610 620 630 640 650 660 NSVHGNSEFI HLAPINEITT IPPLPPRSVA LNPRQKIPCK LVSKTSISHD VRLFRFEMPS 670 680 690 700 710 720 KNQLLGLPVG KHIFLCATID GKLCMRAYTP TSSVEEVGFF DLLIKVYFKD VHPKFPNGGL 730 740 750 760 770 780 MSQYLESLSI GSMLDVKGPL GHIEYTGRGN FTVNGKSRFA KRLAMLAGGT GITPIYQVAQ 790 800 810 820 830 840 AILKDPEDLT EMHVVYANRT EDDILLREEL DTWAKEHCER FKVWYVVETA KEGWGYGVGF 850 860 870 880 890 ITEAIMREHL PEASSDSLAM TCGPPPMIQF AVQPNLEKMG YDIKNDLLVF

References

[1]	Jensen P.E., Hoff T., Stummann B.M., Henningsen K.W. Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: cv. Saxa.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U01029 Unassigned DNA. Translation: AAA95940.1.
PIR	T11805.
3D structure databases
HSSP	HSSP built from PDB template 2CND based on UniProtKB P17571.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.7.1.1. 8.
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_PHAVU

Accession

Primary (citable) accession number: P39866

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)