UniProtKB - Q05531 (NIA_USTMA)
Protein
Nitrate reductase [NADPH]
Gene
NAR1
Organism
Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus)
Status
Functioni
Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
Catalytic activityi
- EC:1.7.1.3
Cofactori
Protein has several cofactor binding sites:- FADBy similarityNote: Binds 1 FAD per subunit.By similarity
- hemeBy similarityNote: Binds 1 heme group per subunit. The heme group is called cytochrome b-557.By similarity
- Mo-molybdopterinBy similarityNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.By similarity
: nitrate reduction (assimilation) Pathwayi
This protein is involved in the pathway nitrate reduction (assimilation), which is part of Nitrogen metabolism.View all proteins of this organism that are known to be involved in the pathway nitrate reduction (assimilation) and in Nitrogen metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 184 | MolybdenumBy similarity | 1 | |
Metal bindingi | 622 | Iron (heme axial ligand)PROSITE-ProRule annotation | 1 | |
Metal bindingi | 645 | Iron (heme axial ligand)PROSITE-ProRule annotation | 1 | |
Binding sitei | 768 | FAD; via carbonyl oxygenBy similarity | 1 | |
Binding sitei | 780 | FAD; via pi-pi stackingBy similarity | 1 | |
Binding sitei | 841 | FADBy similarity | 1 | |
Binding sitei | 844 | FADBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 746 – 749 | FADBy similarity | 4 | |
Nucleotide bindingi | 763 – 767 | FADBy similarity | 5 | |
Nucleotide bindingi | 784 – 786 | FADBy similarity | 3 | |
Nucleotide bindingi | 952 – 961 | NADPBy similarity | 10 |
GO - Molecular functioni
- FAD binding Source: UniProtKB
- heme binding Source: InterPro
- molybdenum ion binding Source: UniProtKB
- molybdopterin cofactor binding Source: InterPro
- nitrate reductase (NADPH) activity Source: UniProtKB-EC
GO - Biological processi
- nitrate assimilation Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Nitrate assimilation |
Ligand | FAD, Flavoprotein, Heme, Iron, Metal-binding, Molybdenum, NADP |
Enzyme and pathway databases
UniPathwayi | UPA00653 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:NAR1 ORF Names:UMAG_03847 |
Organismi | Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) |
Taxonomic identifieri | 237631 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Basidiomycota › Ustilaginomycotina › Ustilaginomycetes › Ustilaginales › Ustilaginaceae › Ustilago › |
Proteomesi |
|
Organism-specific databases
VEuPathDBi | FungiDB:UMAG_03847 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000166048 | 1 – 983 | Nitrate reductase [NADPH]Add BLAST | 983 |
Expressioni
Inductioni
Its expression is highly regulated and responds rapidly to nitrate induction and to ammonium ion repression.
Interactioni
Subunit structurei
Homodimer.
By similarityProtein-protein interaction databases
STRINGi | 5270.UM03847P0 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 585 – 662 | Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd BLAST | 78 | |
Domaini | 688 – 815 | FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST | 128 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 4 – 46 | Ser-richAdd BLAST | 43 | |
Compositional biasi | 936 – 939 | Poly-Pro | 4 |
Sequence similaritiesi
Belongs to the nitrate reductase family.Curated
Phylogenomic databases
eggNOGi | KOG0534, Eukaryota KOG0535, Eukaryota KOG0537, Eukaryota |
HOGENOMi | CLU_003827_4_0_1 |
InParanoidi | Q05531 |
OMAi | ALMPGGW |
OrthoDBi | 166846at2759 |
Family and domain databases
Gene3Di | 3.10.120.10, 1 hit 3.40.50.80, 1 hit 3.90.420.10, 1 hit |
InterProi | View protein in InterPro IPR001834, CBR-like IPR008333, Cbr1-like_FAD-bd_dom IPR001199, Cyt_B5-like_heme/steroid-bd IPR036400, Cyt_B5-like_heme/steroid_sf IPR018506, Cyt_B5_heme-BS IPR017927, FAD-bd_FR_type IPR001709, Flavoprot_Pyr_Nucl_cyt_Rdtase IPR039261, FNR_nucleotide-bd IPR014756, Ig_E-set IPR005066, MoCF_OxRdtse_dimer IPR008335, Mopterin_OxRdtase_euk IPR001433, OxRdtase_FAD/NAD-bd IPR000572, OxRdtase_Mopterin-bd_dom IPR036374, OxRdtase_Mopterin-bd_sf IPR022407, OxRdtase_Mopterin_BS IPR017938, Riboflavin_synthase-like_b-brl |
Pfami | View protein in Pfam 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 |
PRINTSi | PR00406, CYTB5RDTASE PR00363, CYTOCHROMEB5 PR00407, EUMOPTERIN PR00371, FPNCR |
SMARTi | View protein in SMART SM01117, Cyt-b5, 1 hit |
SUPFAMi | SSF52343, SSF52343, 1 hit SSF55856, SSF55856, 1 hit SSF56524, SSF56524, 1 hit SSF63380, SSF63380, 1 hit SSF81296, SSF81296, 1 hit |
PROSITEi | View protein in PROSITE PS00191, CYTOCHROME_B5_1, 1 hit PS50255, CYTOCHROME_B5_2, 1 hit PS51384, FAD_FR, 1 hit PS00559, MOLYBDOPTERIN_EUK, 1 hit |
i Sequence
Sequence statusi: Complete.
Q05531-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTISTTSSST SSKTSSEKGD DLKGFSSSSS PASSRSSSAT TPEPSSPTVL
60 70 80 90 100
AAKTIESIDP FQPRKDYNEN VLPAIPATEA VQPLTSDANT PDHWIARDER
110 120 130 140 150
MIRLTGKHPF NSEAPLSELF SKGFLTPQNL FYVRSHGDTP RVTREQAENW
160 170 180 190 200
KLKVHGLVEQ EVELSIKDLK EKFPTVTLPI TLVCAGNRRK EQNMVAKGLG
210 220 230 240 250
FNWGAAGVST GLFTGVYLAD ILDYCKPKNP LLSSFPSYDV AVPGRARHVV
260 270 280 290 300
FEGADELPKG KYGTSQRLNW ALDRCKGMLI AWGLNGEDLS PDHGYPLRLV
310 320 330 340 350
VPGQIGGRMV KWLERIEVSD RESQHHLHFH DNKVLPTEVT ADQARSEMHW
360 370 380 390 400
WYDPKYIIND LNVNAAICSP DHDQVVNVAE PSTSSPQMLP LEGYAYTGGG
410 420 430 440 450
RRIHRVEISL DDGHSWKCAS IHYPEDLYRM YPIQGHEYFG TLDLSATEMS
460 470 480 490 500
FSWCFWRLDV DVQADIIAKD VKVISVRALD EGLATMPRDM YWNATSMMNS
510 520 530 540 550
WWFRVAVHRE GENGNQIRFE HPTLAGNAPG GWMQRMNEAG LNPRYPQFGE
560 570 580 590 600
AKAVESCKTD ANTLAAAKEA KVDPKAIMID PSKADTIITA ADLAAHGDGE
610 620 630 640 650
GPEPWFVVHG HVYDGTGFLK DHPGGDQSIR LVAGEDATED FMAIHSMDAK
660 670 680 690 700
KMLRDFHLGR LEKQDAAPPA ATTEGEVLDL SKPFLDPKKW RATRLVSKQI
710 720 730 740 750
ISPDARIFRF ALGSEDQELG LPVGQHVFVR VRSKNARTGE TEMVQRAYTP
760 770 780 790 800
YSGNTQRGFL DILIKVYFPS DAAATSAPAF EGGKMTMLLE KIDVSSPSDD
810 820 830 840 850
LTIELKGPLG SFTYLGQQQI RWKPASAVRR VRKLAMIAGG SGITPIWSTL
860 870 880 890 900
KAIADEVLDA SNPSSPALDP IQIWIVYGNR TEQDILIREE LERLRVALKG
910 920 930 940 950
NLKVWHVLSN CTPENEANWS MGRGHITANV LRTHLPPPPA KPASEDELED
960 970 980
TLALVCGPPP MEKAVSDGLK QLGWDLQRCV VFF
Sequence cautioni
The sequence CAA47918 differs from that shown. Reason: Frameshift.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 5 | T → S in CAA47918 (PubMed:8370542).Curated | 1 | |
Sequence conflicti | 18 – 20 | KGD → NP in CAA47918 (PubMed:8370542).Curated | 3 | |
Sequence conflicti | 49 | V → I in CAA47918 (PubMed:8370542).Curated | 1 | |
Sequence conflicti | 136 | H → Q in CAA47918 (PubMed:8370542).Curated | 1 | |
Sequence conflicti | 178 – 179 | LP → PT in CAA47918 (PubMed:8370542).Curated | 2 | |
Sequence conflicti | 243 – 244 | PG → LD in CAA47918 (PubMed:8370542).Curated | 2 | |
Sequence conflicti | 306 | G → S in CAA47918 (PubMed:8370542).Curated | 1 | |
Sequence conflicti | 333 | K → Q in CAA47918 (PubMed:8370542).Curated | 1 | |
Sequence conflicti | 365 | A → S in CAA47918 (PubMed:8370542).Curated | 1 | |
Sequence conflicti | 387 | Q → E in CAA47918 (PubMed:8370542).Curated | 1 | |
Sequence conflicti | 414 | H → R in CAA47918 (PubMed:8370542).Curated | 1 | |
Sequence conflicti | 463 | Q → E in CAA47918 (PubMed:8370542).Curated | 1 | |
Sequence conflicti | 482 | G → V in CAA47918 (PubMed:8370542).Curated | 1 | |
Sequence conflicti | 486 | M → Q in CAA47918 (PubMed:8370542).Curated | 1 | |
Sequence conflicti | 506 | Missing in CAA47918 (PubMed:8370542).Curated | 1 | |
Sequence conflicti | 549 | G → V in CAA47918 (PubMed:8370542).Curated | 1 | |
Sequence conflicti | 572 – 573 | VD → WV in CAA47918 (PubMed:8370542).Curated | 2 | |
Sequence conflicti | 612 | V → L in CAA47918 (PubMed:8370542).Curated | 1 | |
Sequence conflicti | 636 | D → DD in CAA47918 (PubMed:8370542).Curated | 1 | |
Sequence conflicti | 673 – 675 | TEG → ER in CAA47918 (PubMed:8370542).Curated | 3 | |
Sequence conflicti | 726 – 733 | HVFVRVRS → QLCVCRL in CAA47918 (PubMed:8370542).Curated | 8 | |
Sequence conflicti | 741 | T → A in CAA47918 (PubMed:8370542).Curated | 1 | |
Sequence conflicti | 894 – 895 | LR → M in CAA47918 (PubMed:8370542).Curated | 2 | |
Sequence conflicti | 927 | T → S in CAA47918 (PubMed:8370542).Curated | 1 | |
Sequence conflicti | 970 – 971 | KQ → NE in CAA47918 (PubMed:8370542).Curated | 2 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X67687 Genomic DNA Translation: CAA47918.1 Frameshift. AJ315577 Genomic DNA Translation: CAC41650.1 CM003149 Genomic DNA Translation: KIS68266.1 |
PIRi | JN0804 |
RefSeqi | XP_011390279.1, XM_011391977.1 |
Genome annotation databases
EnsemblFungii | KIS68266; KIS68266; UMAG_03847 |
GeneIDi | 23564194 |
KEGGi | uma:UMAG_03847 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X67687 Genomic DNA Translation: CAA47918.1 Frameshift. AJ315577 Genomic DNA Translation: CAC41650.1 CM003149 Genomic DNA Translation: KIS68266.1 |
PIRi | JN0804 |
RefSeqi | XP_011390279.1, XM_011391977.1 |
3D structure databases
SMRi | Q05531 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 5270.UM03847P0 |
Genome annotation databases
EnsemblFungii | KIS68266; KIS68266; UMAG_03847 |
GeneIDi | 23564194 |
KEGGi | uma:UMAG_03847 |
Organism-specific databases
VEuPathDBi | FungiDB:UMAG_03847 |
Phylogenomic databases
eggNOGi | KOG0534, Eukaryota KOG0535, Eukaryota KOG0537, Eukaryota |
HOGENOMi | CLU_003827_4_0_1 |
InParanoidi | Q05531 |
OMAi | ALMPGGW |
OrthoDBi | 166846at2759 |
Enzyme and pathway databases
UniPathwayi | UPA00653 |
Family and domain databases
Gene3Di | 3.10.120.10, 1 hit 3.40.50.80, 1 hit 3.90.420.10, 1 hit |
InterProi | View protein in InterPro IPR001834, CBR-like IPR008333, Cbr1-like_FAD-bd_dom IPR001199, Cyt_B5-like_heme/steroid-bd IPR036400, Cyt_B5-like_heme/steroid_sf IPR018506, Cyt_B5_heme-BS IPR017927, FAD-bd_FR_type IPR001709, Flavoprot_Pyr_Nucl_cyt_Rdtase IPR039261, FNR_nucleotide-bd IPR014756, Ig_E-set IPR005066, MoCF_OxRdtse_dimer IPR008335, Mopterin_OxRdtase_euk IPR001433, OxRdtase_FAD/NAD-bd IPR000572, OxRdtase_Mopterin-bd_dom IPR036374, OxRdtase_Mopterin-bd_sf IPR022407, OxRdtase_Mopterin_BS IPR017938, Riboflavin_synthase-like_b-brl |
Pfami | View protein in Pfam 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 |
PRINTSi | PR00406, CYTB5RDTASE PR00363, CYTOCHROMEB5 PR00407, EUMOPTERIN PR00371, FPNCR |
SMARTi | View protein in SMART SM01117, Cyt-b5, 1 hit |
SUPFAMi | SSF52343, SSF52343, 1 hit SSF55856, SSF55856, 1 hit SSF56524, SSF56524, 1 hit SSF63380, SSF63380, 1 hit SSF81296, SSF81296, 1 hit |
PROSITEi | View protein in PROSITE PS00191, CYTOCHROME_B5_1, 1 hit PS50255, CYTOCHROME_B5_2, 1 hit PS51384, FAD_FR, 1 hit PS00559, MOLYBDOPTERIN_EUK, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | NIA_USTMA | |
Accessioni | Q05531Primary (citable) accession number: Q05531 Secondary accession number(s): A0A0D1DXC6, Q4P7R6, Q96VE8 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 1, 1994 |
Last sequence update: | January 9, 2007 | |
Last modified: | February 10, 2021 | |
This is version 145 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families