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Q05531 (NIA_USTMA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nitrate reductase [NADPH]
Short name=NR
EC=1.7.1.3
Gene names
Name:NAR1
ORF Names:UM03847
OrganismUstilago maydis (strain 521 / FGSC 9021) (Smut fungus)
Taxonomic identifier237631 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Basidiomycota › Ustilaginomycotina › Ustilaginomycetes › Ustilaginales › Ustilaginaceae › Ustilago

Protein attributes

Sequence length983 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 983983Nitrate reductase [NADPH]
PRO_0000166048

Regions

Domain585 – 66278Cytochrome b5 heme-binding
Domain688 – 815128FAD-binding FR-type
Nucleotide binding952 – 96110NADP By similarity
Compositional bias4 – 4643Ser-rich
Compositional bias936 – 9394Poly-Pro

Sites

Metal binding1841Molybdenum-pterin Potential
Metal binding6221Iron (heme axial ligand) By similarity
Metal binding6451Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict51T → S in CAA47918. Ref.1
Sequence conflict18 – 203KGD → NP in CAA47918. Ref.1
Sequence conflict491V → I in CAA47918. Ref.1
Sequence conflict1361H → Q in CAA47918. Ref.1
Sequence conflict178 – 1792LP → PT in CAA47918. Ref.1
Sequence conflict243 – 2442PG → LD in CAA47918. Ref.1
Sequence conflict3061G → S in CAA47918. Ref.1
Sequence conflict3331K → Q in CAA47918. Ref.1
Sequence conflict3651A → S in CAA47918. Ref.1
Sequence conflict3871Q → E in CAA47918. Ref.1
Sequence conflict4141H → R in CAA47918. Ref.1
Sequence conflict4631Q → E in CAA47918. Ref.1
Sequence conflict4821G → V in CAA47918. Ref.1
Sequence conflict4861M → Q in CAA47918. Ref.1
Sequence conflict5061Missing in CAA47918. Ref.1
Sequence conflict5491G → V in CAA47918. Ref.1
Sequence conflict572 – 5732VD → WV in CAA47918. Ref.1
Sequence conflict6121V → L in CAA47918. Ref.1
Sequence conflict6361D → DD in CAA47918. Ref.1
Sequence conflict673 – 6753TEG → ER in CAA47918. Ref.1
Sequence conflict726 – 7338HVFVRVRS → QLCVCRL in CAA47918. Ref.1
Sequence conflict7411T → A in CAA47918. Ref.1
Sequence conflict894 – 8952LR → M in CAA47918. Ref.1
Sequence conflict9271T → S in CAA47918. Ref.1
Sequence conflict970 – 9712KQ → NE in CAA47918. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q05531 [UniParc].

Last modified January 9, 2007. Version 2.
Checksum: E8BF3D172EEB69B9

FASTA983108,826
        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

« Hide

References

« Hide '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 / FGSC 9021.
[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. expand/collapse author list , 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 / FGSC 9021.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X67687 Genomic DNA. Translation: CAA47918.1. Frameshift.
AJ315577 Genomic DNA. Translation: CAC41650.1.
AACP01000131 Genomic DNA. Translation: EAK84753.1.
PIRJN0804.
RefSeqXP_759994.1. XM_754901.1.

3D structure databases

ProteinModelPortalQ05531.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiUM03847T0; UM03847P0; UM03847.
GeneID3631940.
KEGGuma:UM03847.1.

Phylogenomic databases

eggNOGfuNOG06256.
HOGENOMHBG326850.
OMARFEHPTQ.
OrthoDBEOG43JGCT.

Family and domain databases

InterProIPR001199. Cyt_B5.
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.
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]
Gene3DG3DSA: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.
KOK10534.
PfamPF00173. 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]
PRINTSPR00406. CYTB5RDTASE.
PR00363. CYTOCHROMEB5.
PR00407. EUMOPTERIN.
PR00371. FPNCR.
SUPFAMSSF55856. Cyt_B5. 1 hit.
SSF81296. Ig_E-set. 1 hit.
SSF56524. Oxidored_molyb. 1 hit.
SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITEPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS51384. FAD_FR. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNIA_USTMA
AccessionPrimary (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: December 14, 2011
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents