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P36842

- NIA_LEPMC

UniProt

P36842 - NIA_LEPMC

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
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      Previous versions | rss
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    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

    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

    MSVTTQQPAV VPLPSSPRLP IESHAGPRST QLPPSPPETV NGDDPKSITS    50
    TPAEPDFPLP PPANPKPQVL DIDKPTPDAH VPRDPRLIRL TGVHPFNTEP 100
    PLTDLYNEGF LTSPELFYVR NHGAVPEVQD EECLDWEFSI EGMVANPLKI 150
    TLRQLLEEYE NVTYPVTLVC AGNRRKEQNV VRKSKGFAWG AAGVSTALFT 200
    GVVMKDVIER AKPLRKAKYV CMEGADKLPN GYYGTSVKLN WVMDPNRGIM 250
    LAHKMNGENL SLDHGKPLRA VVPGQIGGRS VKWLKKLIVT AEPSDNWYHI 300
    YDNRVLPTMV DPDEAAKNPK WWMDERYAIY DLSPNSAIAF PAHEEKVVLA 350
    SAENSYNVRG YAYSGGGRRI TRCEVSLNKG KNWRLANIDY AEDKYRDFEG 400
    RELFGARLDM DWRETSFCWC FWNLDIATAE LRDANDILVR AMDEAMCIQP 450
    RDMYWSVLGM MNNPWYRITI HHEGDVLRFE HPTQPALIPG GWMERVKKAG 500
    GNLTNGQWGE QIEGQELENT AVEEVKEIKM TKDGVNRIVE LDELKWHESA 550
    EYPWFVVNDE VYDGTSFLEG HPGGAQSIIS AAGLDASDEF MAIHSETAKA 600
    MMPAYHIGTL SPTASKQLSL EEPTSKQASS SSLRPTFLDS RTWSKALLSS 650
    KTKVSWDTRI FRFKLDHASQ TLGLPTGQHL MIRLRDPVTR EAIIRSYTPI 700
    SQISEQGFCD VLIKIYADAP GREGGKMTKA LDSIPCGHWV DMKGPIGKFE 750
    YLGKGVCSIN GNERRVRSMK MICGGSGITP IYQVLRAILQ DSADSTHCTV 800
    LNGNRLEEDI LCREDLDRFA EENGERCTLV HTLTQAAEGW TGRRGRIGEE 850
    LLKEFCGTEE DGLVLVCGPE GLERSVKGLL SGMAWRDDDV IFF 893
    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