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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi284 – 2841Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi307 – 3071Iron (heme axial ligand)PROSITE-ProRule annotation
Sitei593 – 5931Necessary for efficient electron Transfer

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi593 – 5931C → S: Reduction of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 621›621Nitrate reductase [NADH]PRO_0000166062Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi138 – 138InterchainSequence 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

1
621
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi364 – 37512Combined sources
Beta strandi378 – 3847Combined sources
Beta strandi399 – 4068Combined sources
Beta strandi409 – 4157Combined sources
Beta strandi425 – 4328Combined sources
Beta strandi436 – 4383Combined sources
Helixi447 – 4548Combined sources
Beta strandi460 – 4678Combined sources
Beta strandi469 – 4713Combined sources
Beta strandi474 – 4763Combined sources
Beta strandi478 – 4803Combined sources
Beta strandi483 – 4853Combined sources
Beta strandi488 – 4958Combined sources
Helixi496 – 4983Combined sources
Helixi499 – 51113Combined sources
Turni512 – 5154Combined sources
Beta strandi519 – 5279Combined sources
Helixi529 – 5313Combined sources
Helixi535 – 54410Combined sources
Turni546 – 5483Combined sources
Beta strandi549 – 5568Combined sources
Helixi561 – 5633Combined sources
Beta strandi567 – 5715Combined sources
Helixi574 – 5807Combined sources
Beta strandi585 – 5939Combined sources
Helixi596 – 6005Combined sources
Turni601 – 6033Combined sources
Helixi604 – 6085Combined sources
Turni609 – 6113Combined sources
Helixi614 – 6174Combined sources
Beta strandi618 – 6203Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CNEX-ray3.00A352-621[»]
1CNFX-ray2.70A352-621[»]
2CNDX-ray2.50A352-621[»]
ProteinModelPortaliP17571.
SMRiP17571. Positions 363-621.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17571.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini249 – 32476Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini361 – 473113FAD-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

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)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1CNEX-ray3.00A352-621[»]
1CNFX-ray2.70A352-621[»]
2CNDX-ray2.50A352-621[»]
ProteinModelPortaliP17571.
SMRiP17571. Positions 363-621.
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...

Publicationsi

  1. "cDNA clones for corn leaf NADH: nitrate reductase and chloroplast NAD(P)(+): glyceraldehyde-3-phosphate dehydrogenase."
    Gowri G., Campbell W.H.
    Plant Physiol. 90:792-798(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. W64 X W128E.
    Tissue: Leaf.
  2. "High-level expression in Escherichia coli of the catalytically active flavin domain of corn leaf NADH:nitrate reductase and its comparison to human NADH:cytochrome B5 reductase."
    Hyde G.E., Campbell W.H.
    Biochem. Biophys. Res. Commun. 168:1285-1291(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 389-390; 405-406 AND 414-417, CHARACTERIZATION.
    Strain: cv. W64 X W128E.
    Tissue: Leaf.
  3. "The sequence of squash NADH:nitrate reductase and its relationship to the sequences of other flavoprotein oxidoreductases. A family of flavoprotein pyridine nucleotide cytochrome reductases."
    Hyde G.E., Crawford N.M., Campbell W.H.
    J. Biol. Chem. 266:23542-23547(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SECONDARY STRUCTURE OF FAD DOMAIN.
  4. "Identification of an 'essential' cysteine of nitrate reductase via mutagenesis of its recombinant cytochrome b reductase domain."
    Dwivedi U.N., Shiraishi N., Campbell W.H.
    J. Biol. Chem. 269:13785-13791(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-593.
  5. "Crystal structure of the FAD-containing fragment of corn nitrate reductase at 2.5-A resolution: relationship to other flavoprotein reductases."
    Lu G., Campbell W.H., Schneider G., Lindqvist Y.
    Structure 2:809-821(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF FAD DOMAIN.
  6. "Structural studies on corn nitrate reductase: refined structure of the cytochrome b reductase fragment at 2.5 A, its ADP complex and an active-site mutant and modeling of the cytochrome b domain."
    Lu G., Lindqvist Y., Schneider G., Dwivedi U., Campbell W.H.
    J. Mol. Biol. 248:931-948(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 232-501.

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: June 8, 2016
This is version 131 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.