Nitrate reductase [NADH] 1 - Oryza sativa subsp. japonica (Rice)

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P16081 (NIA1_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 98. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Nitrate reductase [NADH] 1
Short name=NR1
EC=1.7.1.1

Gene names

Name:	NIA1
Ordered Locus Names:	Os08g0468100, LOC_Os08g36480
ORF Names:	P0470B03.25

Organism

Oryza sativa subsp. japonica (Rice)

Taxonomic identifier

39947 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza

Protein attributes

Sequence length	916 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.
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
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro molybdenum ion binding Inferred from electronic annotation. Source: InterPro 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 – 916

916

Nitrate reductase [NADH] 1

PRO_0000166065

Regions

Domain

541 – 616

Cytochrome b5 heme-binding

Domain

656 – 768

113

FAD-binding FR-type

Sites

Metal binding

192

Molybdenum-pterin Potential

Metal binding

246

Molybdenum-pterin Potential

Metal binding

576

Iron (heme axial ligand) By similarity

Metal binding

599

Iron (heme axial ligand) By similarity

Amino acid modifications

Disulfide bond

431

Interchain Potential

Experimental info

Sequence conflict

D → N in CAA33817. Ref.1

Sequence conflict

106

I → T in CAA33817. Ref.1

Sequence conflict

129

R → E in CAA33817. Ref.1

Sequence conflict

145

R → A in CAA33817. Ref.1

Sequence conflict

297

R → G in AK121810. Ref.3

Sequence conflict

370

H → Y in CAA33817. Ref.1

Sequence conflict

433

C → R in CAA33817. Ref.1

Sequence conflict

436

S → P in CAA33817. Ref.1

Sequence conflict

442

L → F in CAA33817. Ref.1

Sequence conflict

452

V → A in CAA33817. Ref.1

Sequence conflict

581

D → N in AK121810. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P16081 [UniParc].

Last modified May 30, 2006. Version 3.
Checksum: 844D2A0D537E629D
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FASTA

916

101,513

        10         20         30         40         50         60 
MAASVQPRQF GHLEPGSAPV RGAASSNGAK AYPPANGIPR RADSPVRGCG FPPLVSPPPR 

        70         80         90        100        110        120 
KPPSDGSDDE EEEQEDWREL YGSHLQLEVE PPVRDARDEG TADAWIERNP SLIRLTGKHP 

       130        140        150        160        170        180 
LNCEPPLARL MHHGFITPAA LHYVRNHGAV PRGDWSTWTV DVTGLVKRPM RLTMDELVNG 

       190        200        210        220        230        240 
FPAVEIPVTL VCAGNRRKEQ NMVQQTVGFN WGAAGVSTSV WRGARLRDVL RRCGIMPSKG 

       250        260        270        280        290        300 
GALNVCFEGA EDLPGGGGSK YGTSITRQWA LDPSRDIMLA YMQNGEPLLP DHGFPVRAII 

       310        320        330        340        350        360 
PGCIGGRMVK WVKRIIVTTA ESDNYYHYKD NRVLPSHVDA ELANADAWWY KPEYIINELN 

       370        380        390        400        410        420 
VNSVITTPGH DEILPINGIT TQRGYTMKGY AYSGGGKRIT RVEVTLDGGE TWLVCVLDLP 

       430        440        450        460        470        480 
EKPTKYGKHW CWCFWSVEVE VLDLLGAKEI AVRAWDQSHN TQPEKLIWNL MGMMNNCWFK 

       490        500        510        520        530        540 
VKVNVCRPHK GEIGLVFEHP TQPGNQTGGW MARQKHLETA EAAAPGLKRS TSTPFMNTTD 

       550        560        570        580        590        600 
GKQFTMSEVR KHSSQDSAWI VVHGHVYDCT AFLKDHPGGA DSILINAGTD CTEEFDAIHS 

       610        620        630        640        650        660 
DKAKALLDTY RIGELITTGA GYSSDNSVHG ASNLSQLAPI REAIKAPAPV ALSSPRDKVP 

       670        680        690        700        710        720 
CQLVDKKELS RDVRLFRFAL PSSDQVLGLP VGKHIFVCAS IEGKLCMRAY TPTSMVDEVG 

       730        740        750        760        770        780 
HFDLLIKVYF KNEHPKFPDG GLMTQYLDSL PVGAYIDVKG PLGHVEYTGR GEFVINGKPR 

       790        800        810        820        830        840 
NARRLAMIAG GSGITPMYQV IQSVLRDQPE DTTEMHLVYA NRTEDDILLR DELDRWAAEY 

       850        860        870        880        890        900 
PDRLKVWYVI DQVKRPEEGW KYGVGFVTEE VLREHVPEGG DDTLALACGP PPMIKFAVSP 

       910 
NLEKMKYDMA NSFIVF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of rice nitrate reductase genes." Cheng C., Dewdney J., Nam H., den Boer B.G.W., Goodman H.M., Choi H.K., Kleinhofs A., An G. Plant Mol. Biol. 13:731-733(1989) [PubMed: 2491689] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Biggs M-201.
[2]	"The map-based sequence of the rice genome." International rice genome sequencing project (IRGSP) Nature 436:793-800(2005) [PubMed: 16100779] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[3]	"Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice." The rice full-length cDNA consortium Science 301:376-379(2003) [PubMed: 12869764] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Nipponbare.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X15819, X15820 Genomic DNA. Translation: CAA33817.2. AP004585 Genomic DNA. Translation: BAD09558.1. AK121810 mRNA. No translation available.
PIR	S07554.
RefSeq	NP_001062006.1. NM_001068541.1.
UniGene	Os.4717.
3D structure databases
ProteinModelPortal	P16081.
SMR	P16081. Positions 658-916.
ModBase	Search...
Protein-protein interaction databases
STRING	P16081.
Proteomic databases
PRIDE	P16081.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	LOC_Os08g36480.1; LOC_Os08g36480.1; LOC_Os08g36480.
GeneID	4345795.
KEGG	osa:4345795.
Organism-specific databases
Gramene	P16081.
Phylogenomic databases
OMA	RFEHPTQ.
PhylomeDB	P16081.
ProtClustDB	PLN02252.
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_dom. IPR022407. OxRdtase_Mopterin_BS. 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.
KO	K00360.
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.
SUPFAM	SSF55856. Cyt_B5. 1 hit. SSF81296. Ig_E-set. 1 hit. SSF56524. Oxidored_molyb. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
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

NIA1_ORYSJ

Accession

Primary (citable) accession number: P16081
Secondary accession number(s): Q6ZC37

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	May 30, 2006
Last modified:	November 16, 2011
This is version 98 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Oryza sativa (rice)

Index of Oryza sativa entries and their corresponding gene designations

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents