Reviewed, UniProtKB/Swiss-Prot Q05531 (NIA_USTMA)

Names and origin

Protein names

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

Gene names

Name:	NAR1
ORF Names:	UM03847

Organism

Ustilago maydis (Smut fungus) [Complete proteome]

Taxonomic identifier

5270 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Ustilaginomycotina › Ustilaginomycetes › Ustilaginales › Ustilaginaceae › Ustilago

Protein attributes

Sequence length	983 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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 per subunit. Binds 1 heme group per subunit. The heme group is called cytochrome b-557. Binds 1 molybdenum (molybdopterin) per subunit.
Pathway	Nitrogen metabolism; nitrate reduction (assimilation).
Subunit structure	Homodimer By similarity.
Induction	Its expression is highly regulated and responds rapidly to nitrate induction and to ammonium ion repression.
Sequence similarities	Belongs to the nitrate reductase family. Contains 1 cytochrome b5 heme-binding domain. Contains 1 FAD-binding FR-type domain.
Sequence caution	The sequence CAA47918.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
Biological process	Nitrate assimilation
Ligand	FAD Flavoprotein Heme Iron Metal-binding Molybdenum NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
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	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 – 983	983	Nitrate reductase [NADPH]		PRO_0000166048
Regions
	Domain	585 – 662	78	Cytochrome b5 heme-binding
	Domain	688 – 815	128	FAD-binding FR-type
	Nucleotide binding	952 – 961	10	NADP By similarity
	Compositional bias	4 – 46	43	Ser-rich
	Compositional bias	936 – 939	4	Poly-Pro
Sites
	Metal binding	184	1	Molybdenum-pterin Potential
	Metal binding	622	1	Iron (heme axial ligand) By similarity
	Metal binding	645	1	Iron (heme axial ligand) By similarity
Experimental info
	Sequence conflict	5	1	T → S in CAA47918. Ref.1
	Sequence conflict	18 – 20	3	KGD → NP in CAA47918. Ref.1
	Sequence conflict	49	1	V → I in CAA47918. Ref.1
	Sequence conflict	136	1	H → Q in CAA47918. Ref.1
	Sequence conflict	178 – 179	2	LP → PT in CAA47918. Ref.1
	Sequence conflict	243 – 244	2	PG → LD in CAA47918. Ref.1
	Sequence conflict	306	1	G → S in CAA47918. Ref.1
	Sequence conflict	333	1	K → Q in CAA47918. Ref.1
	Sequence conflict	365	1	A → S in CAA47918. Ref.1
	Sequence conflict	387	1	Q → E in CAA47918. Ref.1
	Sequence conflict	414	1	H → R in CAA47918. Ref.1
	Sequence conflict	463	1	Q → E in CAA47918. Ref.1
	Sequence conflict	482	1	G → V in CAA47918. Ref.1
	Sequence conflict	486	1	M → Q in CAA47918. Ref.1
	Sequence conflict	506	1	Missing in CAA47918. Ref.1
	Sequence conflict	549	1	G → V in CAA47918. Ref.1
	Sequence conflict	572 – 573	2	VD → WV in CAA47918. Ref.1
	Sequence conflict	612	1	V → L in CAA47918. Ref.1
	Sequence conflict	636	1	D → DD in CAA47918. Ref.1
	Sequence conflict	673 – 675	3	TEG → ER in CAA47918. Ref.1
	Sequence conflict	726 – 733	8	HVFVRVRS → QLCVCRL in CAA47918. Ref.1
	Sequence conflict	741	1	T → A in CAA47918. Ref.1
	Sequence conflict	894 – 895	2	LR → M in CAA47918. Ref.1
	Sequence conflict	927	1	T → S in CAA47918. Ref.1
	Sequence conflict	970 – 971	2	KQ → NE in CAA47918. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q05531-1 [UniParc]. Last modified January 9, 2007. Version 2. Checksum: E8BF3D172EEB69B9	FASTA	983	108,826
	10 20 30 40 50 60 MTISTTSSST SSKTSSEKGD DLKGFSSSSS PASSRSSSAT TPEPSSPTVL AAKTIESIDP 70 80 90 100 110 120 FQPRKDYNEN VLPAIPATEA VQPLTSDANT PDHWIARDER MIRLTGKHPF NSEAPLSELF 130 140 150 160 170 180 SKGFLTPQNL FYVRSHGDTP RVTREQAENW KLKVHGLVEQ EVELSIKDLK EKFPTVTLPI 190 200 210 220 230 240 TLVCAGNRRK EQNMVAKGLG FNWGAAGVST GLFTGVYLAD ILDYCKPKNP LLSSFPSYDV 250 260 270 280 290 300 AVPGRARHVV FEGADELPKG KYGTSQRLNW ALDRCKGMLI AWGLNGEDLS PDHGYPLRLV 310 320 330 340 350 360 VPGQIGGRMV KWLERIEVSD RESQHHLHFH DNKVLPTEVT ADQARSEMHW WYDPKYIIND 370 380 390 400 410 420 LNVNAAICSP DHDQVVNVAE PSTSSPQMLP LEGYAYTGGG RRIHRVEISL DDGHSWKCAS 430 440 450 460 470 480 IHYPEDLYRM YPIQGHEYFG TLDLSATEMS FSWCFWRLDV DVQADIIAKD VKVISVRALD 490 500 510 520 530 540 EGLATMPRDM YWNATSMMNS WWFRVAVHRE GENGNQIRFE HPTLAGNAPG GWMQRMNEAG 550 560 570 580 590 600 LNPRYPQFGE AKAVESCKTD ANTLAAAKEA KVDPKAIMID PSKADTIITA ADLAAHGDGE 610 620 630 640 650 660 GPEPWFVVHG HVYDGTGFLK DHPGGDQSIR LVAGEDATED FMAIHSMDAK KMLRDFHLGR 670 680 690 700 710 720 LEKQDAAPPA ATTEGEVLDL SKPFLDPKKW RATRLVSKQI ISPDARIFRF ALGSEDQELG 730 740 750 760 770 780 LPVGQHVFVR VRSKNARTGE TEMVQRAYTP YSGNTQRGFL DILIKVYFPS DAAATSAPAF 790 800 810 820 830 840 EGGKMTMLLE KIDVSSPSDD LTIELKGPLG SFTYLGQQQI RWKPASAVRR VRKLAMIAGG 850 860 870 880 890 900 SGITPIWSTL KAIADEVLDA SNPSSPALDP IQIWIVYGNR TEQDILIREE LERLRVALKG 910 920 930 940 950 960 NLKVWHVLSN CTPENEANWS MGRGHITANV LRTHLPPPPA KPASEDELED TLALVCGPPP 970 980 MEKAVSDGLK QLGWDLQRCV VFF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Ustilago maydis nar1 gene encoding nitrate reductase activity: sequence and transcriptional regulation." Banks G.R., Holden D.W., Kanuga N., Shelton P., Spanos A. Gene 131:69-78(1993) [PubMed: 8370542] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 521.
[2]	"Identification of genes in the bW/bE regulatory cascade in Ustilago maydis." Brachmann A., Weinzierl G., Kaemper J., Kahmann R. Mol. Microbiol. 42:1047-1063(2001) [PubMed: 11737646] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: FBD11.
[3]	"Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis." Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J. , Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L., Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W. Nature 444:97-101(2006) [PubMed: 17080091] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 521.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X67687 Genomic DNA. Translation: CAA47918.1. Frameshift. AJ315577 Genomic DNA. Translation: CAC41650.1. AACP01000131 Genomic DNA. Translation: EAK84753.1.
PIR	JN0804.
RefSeq	XP_759994.1.
3D structure databases
HSSP	HSSP built from PDB template 1EUE based on UniProtKB P04166.
ModBase	Search...
Genome annotation databases
GeneID	3631940.
KEGG	uma:UM03847.1.
Phylogenomic databases
OMA	Q05531. SETAKAM.
Enzyme and pathway databases
BRENDA	1.7.1.3. 2320.
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. 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]
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_USTMA

Accession

Primary (citable) accession number: Q05531
Secondary accession number(s): Q4P7R6, Q96VE8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 9, 2007
Last modified:	June 16, 2009
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)