Reviewed, UniProtKB/Swiss-Prot P43100 (NIA_BEABA)

Names and origin

Protein names

Recommended name:
    Nitrate reductase [NADPH]
      Short name=NR
    EC=1.7.1.3

Gene names

Name:

NIA

Organism

Beauveria bassiana (Tritirachium shiotae)

Taxonomic identifier

176275 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Cordycipitaceae › Cordyceps

Protein attributes

Sequence length	894 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
Catalytic activity	Nitrite + NADP+ + H2O = nitrate + NADPH.
Cofactor	Binds 1 FAD. Binds 1 heme group. The heme group is called cytochrome b-557. Binds 1 molybdenum ion.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the nitrate reductase family. Contains 1 cytochrome b5 heme-binding domain. Contains 1 FAD-binding FR-type domain.

Ontologies

Keywords
Biological process	Nitrate assimilation
Ligand	FAD Flavoprotein Heme Iron Metal-binding Molybdenum NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Gene Ontology (GO)
Biological process	nitrate assimilation Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro molybdenum ion binding Inferred from electronic annotation. Source: UniProtKB-KW nitrate reductase (NADPH) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 894	894	Nitrate reductase [NADPH]		PRO_0000166041
Regions
	Domain	535 – 610	76	Cytochrome b5 heme-binding
	Domain	638 – 749	112	FAD-binding FR-type
Sites
	Metal binding	169	1	Molybdenum-pterin Potential
	Metal binding	220	1	Molybdenum-pterin Potential
	Metal binding	570	1	Iron (heme axial ligand) By similarity
	Metal binding	593	1	Iron (heme axial ligand) By similarity
Amino acid modifications
	Disulfide bond	418		Interchain Potential

Sequences

	Sequence		Length	Mass (Da)
	P43100-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: D0ED234BF1B1322B	FASTA	894	99,934
	10 20 30 40 50 60 MAVKSQLGVT YTTKTFPPSP PRTVGNSHAG SDDERDEVDA TPTTPPVEKL GQLLKPYSLP 70 80 90 100 110 120 PTNTPTHVLP EDLKTPDHRV NRDPRLIRLT GVHPFNVEPP LTDLYDEGFL NSENLHYVRN 130 140 150 160 170 180 HGPVPHCPDD ESLNWTFTVD GLVEKPFTIA VRDLIQKYDQ FTYPVTLVCA GNRRKEQNVV 190 200 210 220 230 240 RKSKGFSWGA AGLSTALWTG VPIGALLRMA KPKRAAKYVC FEGADKLPNG YYGTSVKLNW 250 260 270 280 290 300 CMDENRGIMV AHKMNGQSLH PDHGKPVRII IPGQIGGRSV KWLKKITITS EPSDNWYHIY 310 320 330 340 350 360 DNRVLPTTIS PDASANLPDV WKDEKYAIYD LNANSAICYP RHDERLVLAT APDTYKVRGY 370 380 390 400 410 420 AYGGGGKRIT RLEVTLNKGK SWLLAGIHYP EDDYRRAPDG DLLYGGSTDM WWRETCFCWC 430 440 450 460 470 480 FWEIDIPVAD LSAADDIMIR AMDEGMMVQP RDMYWSVLGM MNNPWFRVVI HKEDGALRFE 490 500 510 520 530 540 HPTQPALMPG GWMERVKRRG GNLTNGFWGE KTAAEEEQVL AEPEKEICMT NPKVVRIISL 550 560 570 580 590 600 EELKAHEGEM EPWFVVNGHV YNGTPYLDNH PGGATSIINA AAQDATEEFM TIHSENAKAM 610 620 630 640 650 660 MPQYHIGTLN DAARKALEGS AEESPASDPT RAVFLQPKYW SKAILETKTD VSSDSKIFSF 670 680 690 700 710 720 RLDHAAQSIG LPTGQHLLVR LRDPATREAV IRAYTPLSET HAKGQLDILI KIYRDVPGQP 730 740 750 760 770 780 GGKMTQALDS IPLGHFVDIK GPVGKFEYLG KGHCTVSGTS RHVRRFVMIC AGSGVTPIFQ 790 800 810 820 830 840 VLRAVTSDAQ DGTECLVLDG NRCEKDILCR EELDAMVARA PARTTLLHKL SRPDASWCGL 850 860 870 880 890 RGRMDKEYLE EHIGGFRKSD GREMVLVCGP AALEETVRSV LVEMAWKPED MLFF

References

[1]	Maurer P. Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BB147.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X84950 Genomic DNA. Translation: CAA59336.1.
PIR	S52857.
3D structure databases
HSSP	HSSP built from PDB template 1EUE based on UniProtKB P04166.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.7.1.3. 97823.
Family and domain databases
InterPro	IPR001199. Cyt_B5. IPR018506. Cyt_B5_heme-BS. IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR005066. MoCF_OxRdtse_dimer. IPR008335. Mopterin_OxRdtase_euk. IPR001834. NADH-Cyt_B5_reductase. IPR012137. Nitr_rd_NADH. IPR008333. OxRdtase_FAD-bd. IPR001433. OxRdtase_FAD/NAD_bd. IPR000572. OxRdtase_Mopterin-bd. [Graphical view]
Gene3D	G3DSA:3.10.120.10. Cyt_B5. 1 hit. G3DSA:2.60.40.650. MoCF_oxrdtse_dimer. 1 hit. G3DSA:3.90.420.10. Oxred_molyb_bd. 1 hit.
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. [Graphical view]
PIRSF	PIRSF000233. Nitr_rd_NADH. 1 hit.
PRINTS	PR00406. CYTB5RDTASE. PR00363. CYTOCHROMEB5. PR00407. EUMOPTERIN. PR00371. FPNCR.
ProDom	PD000612. Cyt_B5. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00191. CYTOCHROME_B5_1. 1 hit. PS50255. CYTOCHROME_B5_2. 1 hit. PS51384. FAD_FR. 1 hit. PS00559. MOLYBDOPTERIN_EUK. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NIA_BEABA

Accession

Primary (citable) accession number: P43100

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)