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Protein

Nitrate reductase [NADH] 1

Gene

NIA1

Organism
Phaseolus vulgaris (Kidney bean) (French bean)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.

Catalytic activityi

Nitrite + NAD+ + H2O = nitrate + NADH.

Cofactori

Protein has several cofactor binding sites:
  • FADBy similarityNote: Binds 1 FAD.By similarity
  • hemeBy similarityNote: Binds 1 heme group. The heme group is called cytochrome b-557.By similarity
  • Mo-molybdopterinBy similarityNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi167 – 1671MolybdenumBy similarity
Metal bindingi550 – 5501Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi573 – 5731Iron (heme axial ligand)PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Nitrate assimilation

Keywords - Ligandi

FAD, Flavoprotein, Heme, Iron, Metal-binding, Molybdenum, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrate reductase [NADH] 1 (EC:1.7.1.1)
Short name:
NR-1
Gene namesi
Name:NIA1
Synonyms:NR1
OrganismiPhaseolus vulgaris (Kidney bean) (French bean)
Taxonomic identifieri3885 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaePhaseolus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 881881Nitrate reductase [NADH] 1PRO_0000166067Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi406 – 406InterchainSequence analysis

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP39865.
SMRiP39865. Positions 627-881.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini515 – 59076Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini625 – 737113FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the nitrate reductase family.Curated
Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di2.60.40.650. 1 hit.
3.10.120.10. 1 hit.
3.90.420.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
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]
PfamiPF00173. 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]
PIRSFiPIRSF000233. Nitr_rd_NADH. 1 hit.
PRINTSiPR00406. CYTB5RDTASE.
PR00363. CYTOCHROMEB5.
PR00407. EUMOPTERIN.
PR00371. FPNCR.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
SSF56524. SSF56524. 1 hit.
SSF63380. SSF63380. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS51384. FAD_FR. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39865-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASVEHRPF TSHQHGVVRS FKSYPDVPRP KKLPLPQPLS DSTNDNDEEA
60 70 80 90 100
AVWKELVLKS SAGVEPSIFD PRDDGTSDQW IKRNASMIRL TGKHPFNAEP
110 120 130 140 150
PLPRLMQHGF ITPSPIHYVR SHGPVPHARW EDWTVEVTGL VTRPTCFTME
160 170 180 190 200
QLVNDFPSHE FPATLVCAGN RRKEQNMVKQ SIGFNWGAGG VSTSVWRGVS
210 220 230 240 250
LRSLLKRCGI YSRAKGALHV CFEGAEDLPG GGGSNYGTSL MREVALDPSR
260 270 280 290 300
DIILAYMQNG ELLSPDHGFP VRMIIPGFIG GRMVKWLKRI VVSNQQSQSH
310 320 330 340 350
YHYKDNKLFP SHVDAELANE EDWWYKPEYI INEVNINSVI TTPSHQEILP
360 370 380 390 400
INSWTTQMPY SMRGYAYSGG GRKVTRVEVT LDGGETWQVC SVERLEKPNK
410 420 430 440 450
YGKYWCWCFW SLEVEVLDIL GAKEIAVRAW DEAQNTQPEK LIWNTMGMIN
460 470 480 490 500
NCWFRVKTNV CKPKKGEIGI VFEHPTQPGN QSGGWMAREK QLEKSSESNP
510 520 530 540 550
ILKKSVSSPF MNTATKSYSL SEVRRHNNRD SAWIIVNGHV YDCTRFLKDH
560 570 580 590 600
PGGEDSILLN AGTDCTEEFE AIHSDKAKKM LEDYRIGELM TTDYTSDSSS
610 620 630 640 650
SNNSVHGNSE TTHLAPIREV ALNPREKIPC KLLSKTSISH DVRLLRFALP
660 670 680 690 700
AEDQVMGLPV GNHVFLCATV DEKLCMRAYT PTSSVDEVGF FDLVVKVYFK
710 720 730 740 750
GVHPNFPNGG IMSQHLDSLP IGSVVDVKGP LGHIEYTGRG NFLVHGKPRF
760 770 780 790 800
AKRLTMLAGG TGITPIYQVV QAILKDPEDR TEMYVVYANR TEDDILLKEE
810 820 830 840 850
LDEWAKKHDR LKVWYVLQAN IREGWEYSVG FITESILREH VPLASPDTLA
860 870 880
LTCGPPPMIQ FAVQPNLEKL GYDIQNDLLV F
Length:881
Mass (Da):99,223
Last modified:February 1, 1995 - v1
Checksum:iA212A1288B4EE661
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53603 Genomic DNA. Translation: CAA37672.1.
PIRiS25445.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53603 Genomic DNA. Translation: CAA37672.1.
PIRiS25445.

3D structure databases

ProteinModelPortaliP39865.
SMRiP39865. Positions 627-881.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.40.650. 1 hit.
3.10.120.10. 1 hit.
3.90.420.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
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]
PfamiPF00173. 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]
PIRSFiPIRSF000233. Nitr_rd_NADH. 1 hit.
PRINTSiPR00406. CYTB5RDTASE.
PR00363. CYTOCHROMEB5.
PR00407. EUMOPTERIN.
PR00371. FPNCR.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
SSF56524. SSF56524. 1 hit.
SSF63380. SSF63380. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS51384. FAD_FR. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and expression of a gene encoding a root specific nitrate reductase in bean (Phaseolus vulgaris)."
    Hoff T., Stummann B.M., Henningsen K.W.
    Physiol. Plantarum 82:197-204(1991)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Saxa.
    Tissue: Shoot.

Entry informationi

Entry nameiNIA1_PHAVU
AccessioniPrimary (citable) accession number: P39865
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 11, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.