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Protein

Nitrate reductase [NADH] 2

Gene

NIA2

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)DescriptionActionsGraphical viewLength
Metal bindingi165MolybdenumBy similarity1
Metal bindingi548Iron (heme axial ligand)PROSITE-ProRule annotation1
Metal bindingi571Iron (heme axial ligand)PROSITE-ProRule annotation1

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] 2 (EC:1.7.1.1)
Short name:
NR-2
Gene namesi
Name:NIA2
Synonyms:NR2
OrganismiPhaseolus vulgaris (Kidney bean) (French bean)
Taxonomic identifieri3885 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaePhaseolus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001660681 – 890Nitrate reductase [NADH] 2Add BLAST890

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi404InterchainSequence analysis

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP39866.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini513 – 588Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd BLAST76
Domaini634 – 746FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST113

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.

P39866-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASVGNRQF ATHMNGVVRS CGQDLKPSLP LDFDLDSSSS DDDENDDASY
60 70 80 90 100
LKELVRKANA ETEASVMDPR DEGTADQWVA RNASMVRLTG KHPFNAESPL
110 120 130 140 150
QRLMHHGFIT PVPLHYVRNH GPVPKANWED WTVEITGLVK RPTRFTMDRL
160 170 180 190 200
VREFPHREFP ATLVCAGNRR KEQNMVKKTI GFNWGSAGTS TSVWRGVPVR
210 220 230 240 250
HVLRRCGILT RGKGALHVSF EGAENLPGGG GSKYGTSISR EMAMDPSRDI
260 270 280 290 300
ILAYMQNGEP LAPDHGFPIR MIIPGFIGGR MVKWLKRIVV TEQECESHYH
310 320 330 340 350
YKDNRVLPSH VDPELANEEG WWFKPEYIIN ELNINSVITT PCHDEILPIN
360 370 380 390 400
SWTTQRPYVV RGYAYSGGGR KVTRVEVTLD GGETWHVCTL DHPEKPNKYG
410 420 430 440 450
KYWCWCFWSL EVEVLDLLGT KEIAVRAWDE GLNTQPENLI WNLMGMMNNC
460 470 480 490 500
WFRVKTNVCK PHKGEIGIVF EHPTQPGNQP GGWMAKEKHL EQSQEAKPSL
510 520 530 540 550
KKSVSTPFMN TASKMFSVSE VKKHSSPDSA WIIVHGHVYD CTRFLKDHPG
560 570 580 590 600
GTDSILINAG TDCTEEFDAI HSDKAKKMLE DYRIGELITT GYTSADSSPN
610 620 630 640 650
NSVHGNSEFI HLAPINEITT IPPLPPRSVA LNPRQKIPCK LVSKTSISHD
660 670 680 690 700
VRLFRFEMPS KNQLLGLPVG KHIFLCATID GKLCMRAYTP TSSVEEVGFF
710 720 730 740 750
DLLIKVYFKD VHPKFPNGGL MSQYLESLSI GSMLDVKGPL GHIEYTGRGN
760 770 780 790 800
FTVNGKSRFA KRLAMLAGGT GITPIYQVAQ AILKDPEDLT EMHVVYANRT
810 820 830 840 850
EDDILLREEL DTWAKEHCER FKVWYVVETA KEGWGYGVGF ITEAIMREHL
860 870 880 890
PEASSDSLAM TCGPPPMIQF AVQPNLEKMG YDIKNDLLVF
Length:890
Mass (Da):99,995
Last modified:February 1, 1995 - v1
Checksum:iFC03B96F0139DE1E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01029 Unassigned DNA. Translation: AAA95940.1.
PIRiT11805.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01029 Unassigned DNA. Translation: AAA95940.1.
PIRiT11805.

3D structure databases

ProteinModelPortaliP39866.
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...

Entry informationi

Entry nameiNIA2_PHAVU
AccessioniPrimary (citable) accession number: P39866
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 5, 2016
This is version 91 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.