Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P36842

- NIA_LEPMC

UniProt

P36842 - NIA_LEPMC

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Nitrate reductase [NADPH]

Gene

NIAD

Organism
Leptosphaeria maculans (Blackleg fungus) (Phoma lingam)
Status
Reviewed - Annotation score: 4 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 + NADP+ + H2O = nitrate + NADPH.

Cofactori

Binds 1 FAD.By similarity
Binds 1 heme group. The heme group is called cytochrome b-557 By similarity.By similarity
Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi170 – 1701MolybdenumBy similarity
Metal bindingi571 – 5711Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi594 – 5941Iron (heme axial ligand)PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi863 – 87210NADPBy similarity

GO - Molecular functioni

  1. electron carrier activity Source: InterPro
  2. flavin adenine dinucleotide binding Source: InterPro
  3. heme binding Source: InterPro
  4. iron ion binding Source: InterPro
  5. molybdenum ion binding Source: InterPro
  6. molybdopterin cofactor binding Source: InterPro
  7. nitrate reductase (NADPH) activity Source: UniProtKB-EC

GO - Biological processi

  1. nitrate assimilation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Nitrate assimilation

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrate reductase [NADPH] (EC:1.7.1.3)
Short name:
NR
Gene namesi
Name:NIAD
OrganismiLeptosphaeria maculans (Blackleg fungus) (Phoma lingam)
Taxonomic identifieri5022 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaeLeptosphaeriaceaeLeptosphaeriaLeptosphaeria maculans complex

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 893893Nitrate reductase [NADPH]PRO_0000166045Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi418 – 418InterchainSequence Analysis

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP36842.
SMRiP36842. Positions 61-511.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini536 – 61176Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini641 – 752112FAD-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.
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.

P36842-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSVTTQQPAV VPLPSSPRLP IESHAGPRST QLPPSPPETV NGDDPKSITS
60 70 80 90 100
TPAEPDFPLP PPANPKPQVL DIDKPTPDAH VPRDPRLIRL TGVHPFNTEP
110 120 130 140 150
PLTDLYNEGF LTSPELFYVR NHGAVPEVQD EECLDWEFSI EGMVANPLKI
160 170 180 190 200
TLRQLLEEYE NVTYPVTLVC AGNRRKEQNV VRKSKGFAWG AAGVSTALFT
210 220 230 240 250
GVVMKDVIER AKPLRKAKYV CMEGADKLPN GYYGTSVKLN WVMDPNRGIM
260 270 280 290 300
LAHKMNGENL SLDHGKPLRA VVPGQIGGRS VKWLKKLIVT AEPSDNWYHI
310 320 330 340 350
YDNRVLPTMV DPDEAAKNPK WWMDERYAIY DLSPNSAIAF PAHEEKVVLA
360 370 380 390 400
SAENSYNVRG YAYSGGGRRI TRCEVSLNKG KNWRLANIDY AEDKYRDFEG
410 420 430 440 450
RELFGARLDM DWRETSFCWC FWNLDIATAE LRDANDILVR AMDEAMCIQP
460 470 480 490 500
RDMYWSVLGM MNNPWYRITI HHEGDVLRFE HPTQPALIPG GWMERVKKAG
510 520 530 540 550
GNLTNGQWGE QIEGQELENT AVEEVKEIKM TKDGVNRIVE LDELKWHESA
560 570 580 590 600
EYPWFVVNDE VYDGTSFLEG HPGGAQSIIS AAGLDASDEF MAIHSETAKA
610 620 630 640 650
MMPAYHIGTL SPTASKQLSL EEPTSKQASS SSLRPTFLDS RTWSKALLSS
660 670 680 690 700
KTKVSWDTRI FRFKLDHASQ TLGLPTGQHL MIRLRDPVTR EAIIRSYTPI
710 720 730 740 750
SQISEQGFCD VLIKIYADAP GREGGKMTKA LDSIPCGHWV DMKGPIGKFE
760 770 780 790 800
YLGKGVCSIN GNERRVRSMK MICGGSGITP IYQVLRAILQ DSADSTHCTV
810 820 830 840 850
LNGNRLEEDI LCREDLDRFA EENGERCTLV HTLTQAAEGW TGRRGRIGEE
860 870 880 890
LLKEFCGTEE DGLVLVCGPE GLERSVKGLL SGMAWRDDDV IFF
Length:893
Mass (Da):99,942
Last modified:February 1, 1995 - v2
Checksum:i7686E3C9676DD2EF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U04445 Genomic DNA. Translation: AAA50579.1.
U18793 Genomic DNA. Translation: AAA82740.1.
PIRiS46442.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U04445 Genomic DNA. Translation: AAA50579.1 .
U18793 Genomic DNA. Translation: AAA82740.1 .
PIRi S46442.

3D structure databases

ProteinModelPortali P36842.
SMRi P36842. Positions 61-511.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.60.40.650. 1 hit.
3.10.120.10. 1 hit.
3.90.420.10. 1 hit.
InterProi IPR001199. 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 ]
Pfami 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 ]
PIRSFi PIRSF000233. Nitr_rd_NADH. 1 hit.
PRINTSi PR00406. CYTB5RDTASE.
PR00363. CYTOCHROMEB5.
PR00407. EUMOPTERIN.
PR00371. FPNCR.
SUPFAMi SSF55856. SSF55856. 1 hit.
SSF56524. SSF56524. 1 hit.
SSF63380. SSF63380. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEi PS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS51384. FAD_FR. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Nitrate reductase of the ascomycetous fungus, Leptosphaeria maculans: gene sequence and chromosomal location."
    Williams R.S.B., Davis M.A., Howlett B.J.
    Mol. Gen. Genet. 244:1-8(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Isolate 19.
  2. "The nitrate and nitrite reductase-encoding genes of Leptosphaeria maculans are closely linked and transcribed in the same direction."
    Williams R.S.B., Davis M.A., Howlett B.J.
    Gene 158:153-154(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 886-893.
    Strain: Isolate 19.

Entry informationi

Entry nameiNIA_LEPMC
AccessioniPrimary (citable) accession number: P36842
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 1, 1995
Last modified: October 1, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3