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Protein

Nitrate reductase [NADH]

Gene
N/A
Organism
Zea mays (Maize)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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:
  • FADNote: Binds 1 FAD.
  • hemeNote: Binds 1 heme group. The heme group is called cytochrome b-557.
  • Mo-molybdopterinBy similarityNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi284Iron (heme axial ligand)PROSITE-ProRule annotation1
Metal bindingi307Iron (heme axial ligand)PROSITE-ProRule annotation1
Sitei593Necessary for efficient electron Transfer1

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

Enzyme and pathway databases

BRENDAi1.7.1.1. 6752.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrate reductase [NADH] (EC:1.7.1.1)
Short name:
NR
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogonodaeAndropogoneaeTripsacinaeZea
Proteomesi
  • UP000007305 Componenti: Unplaced

Organism-specific databases

MaizeGDBi25899.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi593C → S: Reduction of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000166062‹1 – 621Nitrate reductase [NADH]Add BLAST›621

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi138InterchainSequence analysis

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP17571.
PRIDEiP17571.

PTM databases

iPTMnetiP17571.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi4577.GRMZM2G568636_P01.

Structurei

Secondary structure

1621
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi364 – 375Combined sources12
Beta strandi378 – 384Combined sources7
Beta strandi399 – 406Combined sources8
Beta strandi409 – 415Combined sources7
Beta strandi425 – 432Combined sources8
Beta strandi436 – 438Combined sources3
Helixi447 – 454Combined sources8
Beta strandi460 – 467Combined sources8
Beta strandi469 – 471Combined sources3
Beta strandi474 – 476Combined sources3
Beta strandi478 – 480Combined sources3
Beta strandi483 – 485Combined sources3
Beta strandi488 – 495Combined sources8
Helixi496 – 498Combined sources3
Helixi499 – 511Combined sources13
Turni512 – 515Combined sources4
Beta strandi519 – 527Combined sources9
Helixi529 – 531Combined sources3
Helixi535 – 544Combined sources10
Turni546 – 548Combined sources3
Beta strandi549 – 556Combined sources8
Helixi561 – 563Combined sources3
Beta strandi567 – 571Combined sources5
Helixi574 – 580Combined sources7
Beta strandi585 – 593Combined sources9
Helixi596 – 600Combined sources5
Turni601 – 603Combined sources3
Helixi604 – 608Combined sources5
Turni609 – 611Combined sources3
Helixi614 – 617Combined sources4
Beta strandi618 – 620Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CNEX-ray3.00A352-621[»]
1CNFX-ray2.70A352-621[»]
2CNDX-ray2.50A352-621[»]
ProteinModelPortaliP17571.
SMRiP17571.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17571.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini249 – 324Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd BLAST76
Domaini361 – 473FAD-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

Phylogenomic databases

eggNOGiKOG0534. Eukaryota.
KOG0535. Eukaryota.
KOG0537. Eukaryota.
COG0543. LUCA.
COG2041. LUCA.

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.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR000572. OxRdtase_Mopterin-bd_dom.
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]
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.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P17571-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GFPVRVIIPG CIGGRMVKWL KRIIVTPAES DNYYHFKDNR VLPSHVDAEL
60 70 80 90 100
ANAEAWWYKP EYIINELNIN SVITTPCHDE ILPINAFTTQ RPYTLKGYAY
110 120 130 140 150
SGGGKKVTRV EVTLDGGETW LVCTDHPEKP TKYGKYWCWC FWSLEVEVLD
160 170 180 190 200
LLSAKEIAVR AWDESLNTQP EKLIWNVMGM MNNCWFRVKT NVCKPHKGEI
210 220 230 240 250
GIVFDHPTLP GNESGGWMAK EKHLETAEAA APGLKRSTST PFMNTTDVGK
260 270 280 290 300
EFTMSEVRKH ASQESAWIVV HGHVYDCTKF LKDHPGGADS ILINAGTDCT
310 320 330 340 350
EEFDAIHSDK AKALLDTYRI GELITTGTGY SSDNSVHGGS VLSHLAPIRR
360 370 380 390 400
AVRAPALSNP REKIHCRLVG KKELSRDVRL FRFSLPSPDQ VLGLPIGKHI
410 420 430 440 450
FVCASIEGKL CMRAYTPTSM VDEIGHFDLL VKVYFKNEHP KFPNGGLMTQ
460 470 480 490 500
YLDSLPVGSY IDVKGPLGHV EYTGRGSFVI NGKQRHASRL AMICGGSGIT
510 520 530 540 550
PMYQIIQAVL RDQPEDHTEM HLVYANRTED DILLRDELDR WAAEYPDRLK
560 570 580 590 600
VWYVIDQVKR PEEGWKYSVG FVTEAVLREH VPEGGDDTLA LACGPPPMIQ
610 620
FAISPNLEKM KYDMANSFVV F
Length:621
Mass (Da):69,773
Last modified:February 1, 1995 - v2
Checksum:iACC276E4ED0FF5D3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27821 mRNA. Translation: AAA03202.1. Sequence problems.
PIRiS19254.
UniGeneiZm.15815.
Zm.1826.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27821 mRNA. Translation: AAA03202.1. Sequence problems.
PIRiS19254.
UniGeneiZm.15815.
Zm.1826.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CNEX-ray3.00A352-621[»]
1CNFX-ray2.70A352-621[»]
2CNDX-ray2.50A352-621[»]
ProteinModelPortaliP17571.
SMRiP17571.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4577.GRMZM2G568636_P01.

PTM databases

iPTMnetiP17571.

Proteomic databases

PaxDbiP17571.
PRIDEiP17571.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MaizeGDBi25899.

Phylogenomic databases

eggNOGiKOG0534. Eukaryota.
KOG0535. Eukaryota.
KOG0537. Eukaryota.
COG0543. LUCA.
COG2041. LUCA.

Enzyme and pathway databases

BRENDAi1.7.1.1. 6752.

Miscellaneous databases

EvolutionaryTraceiP17571.

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.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR000572. OxRdtase_Mopterin-bd_dom.
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]
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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNIA1_MAIZE
AccessioniPrimary (citable) accession number: P17571
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.