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Protein

Nitrogen metabolite repression protein nmrA

Gene

nmrA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be a redox sensor protein. Has much higher affinity for NAD(P) than for NAD(P)H. Has similar affinity for NAD and NADP. Negative transcriptional regulator involved in the post-transcriptional modulation of the GATA-type transcription factor areA, forming part of a system controlling nitrogen metabolite repression (By similarity). Interferes with the interaction between areA and target DNA. Overexpression leads to areA inhibition.By similarity4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei37 – 371NAD or NADP1 Publication
Binding sitei80 – 801NAD or NADP1 Publication
Binding sitei131 – 1311NAD or NADP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 176NAD or NADP1 Publication
Nucleotide bindingi153 – 1564NAD or NADP1 Publication

GO - Molecular functioni

  • NAD+ binding Source: UniProtKB
  • NAD binding Source: UniProtKB
  • NADP+ binding Source: UniProtKB
  • oxidoreductase activity Source: UniProtKB-KW

GO - Biological processi

  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • nitrogen catabolite repression of transcription Source: ASPGD
  • nitrogen catabolite repression of transcription from RNA polymerase II promoter Source: ASPGD
  • regulation of nitrogen utilization Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

NAD, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrogen metabolite repression protein nmrA
Alternative name(s):
Negative-acting nitrogen regulatory protein nmrA
Nitrogen metabolite regulation protein
Gene namesi
Name:nmrA
ORF Names:AN8168
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000000560 Componenti: Chromosome II
  • UP000005890 Componenti: Partially assembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:AN8168.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nucleus Source: ASPGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Displays partial derepression of activities subject to nitrogen metabolic repression.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi12 – 121N → G: 13-fold increase in the Kd for NAD; 2-fold increase in the Kd for NADP and 2-fold increase in the Kd for areA; when associated with G-18. 1 Publication
Mutagenesisi14 – 141T → V: 4-fold increase in the Kd for NAD; 7-fold increase in the Kd for NADP and no change in the Kd for areA. 1 Publication
Mutagenesisi18 – 181A → G: 13-fold increase in the Kd for NAD; 2-fold increase in the Kd for NADP and 2-fold increase in the Kd for areA; when associated with G-12. 1 Publication
Mutagenesisi37 – 371H → W: 4-fold decrease in the Kd for NAD; 24% increase in the Kd for NADP and no change in the Kd for areA. 1 Publication
Mutagenesisi193 – 1931E → Q: No changes in the Kd for NAD and NADP and almost complete loss of affinity for areA; when associated with N-195. 1 Publication
Mutagenesisi195 – 1951D → N: No changes in the Kd for NAD and NADP and almost complete loss of affinity for areA; when associated with Q-193. 1 Publication
Mutagenesisi202 – 2021Q → E: No changes in the Kd for NAD and NADP and 2-fold increase in the Kd for areA; when associated with Y-204. 1 Publication
Mutagenesisi204 – 2041F → Y: No changes in the Kd for NAD and NADP and 2-fold increase in the Kd for areA; when associated with E-202. 1 Publication
Mutagenesisi263 – 2631E → Q: No changes in the Kd for NAD; NADP and areA; when associated with Q-266. 1 Publication
Mutagenesisi266 – 2661E → Q: No changes in the Kd for NAD; NADP and areA; when associated with Q-263. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 352352Nitrogen metabolite repression protein nmrAPRO_0000393568Add
BLAST

Expressioni

Inductioni

Up-regulated in nitrogen-sufficient conditions and down-regulated in nitrogen-limiting conditions.1 Publication

Interactioni

Subunit structurei

Monomer. Interacts with areA.4 Publications

Structurei

Secondary structure

1
352
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 125Combined sources
Helixi16 – 2712Combined sources
Beta strandi32 – 376Combined sources
Helixi42 – 487Combined sources
Beta strandi53 – 586Combined sources
Helixi64 – 718Combined sources
Beta strandi75 – 795Combined sources
Helixi83 – 853Combined sources
Helixi88 – 10215Combined sources
Beta strandi106 – 1127Combined sources
Helixi116 – 1183Combined sources
Beta strandi119 – 1213Combined sources
Turni126 – 1283Combined sources
Helixi129 – 13911Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi145 – 1506Combined sources
Helixi154 – 1563Combined sources
Beta strandi158 – 1614Combined sources
Beta strandi166 – 1694Combined sources
Beta strandi175 – 1817Combined sources
Beta strandi183 – 1853Combined sources
Beta strandi187 – 1904Combined sources
Helixi192 – 20615Combined sources
Helixi208 – 2114Combined sources
Beta strandi215 – 2184Combined sources
Beta strandi220 – 2234Combined sources
Helixi225 – 23612Combined sources
Beta strandi240 – 2445Combined sources
Helixi256 – 26914Combined sources
Helixi280 – 2823Combined sources
Beta strandi283 – 2853Combined sources
Helixi319 – 3246Combined sources
Helixi331 – 3377Combined sources
Helixi339 – 3457Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K6IX-ray1.80A1-352[»]
1K6JX-ray1.80A/B1-352[»]
1K6XX-ray1.50A1-352[»]
1TI7X-ray1.70A1-352[»]
1XGKX-ray1.40A1-352[»]
2VUSX-ray2.60A/B/C/D/E/F/G/H1-352[»]
2VUTX-ray2.30A/B/C/D/E/F/G/H1-352[»]
2VUUX-ray2.80A/B/C/D/E/F/G/H1-352[»]
ProteinModelPortaliQ5AU62.
SMRiQ5AU62. Positions 3-352.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5AU62.

Family & Domainsi

Sequence similaritiesi

Belongs to the NmrA-type oxidoreductase family.Curated

Phylogenomic databases

HOGENOMiHOG000160478.
InParanoidiQ5AU62.
OMAiANGLTWM.
OrthoDBiEOG75TMNQ.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR008030. NmrA-like.
[Graphical view]
PfamiPF05368. NmrA. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5AU62-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQQKKTIAV VNATGRQAAS LIRVAAAVGH HVRAQVHSLK GLIAEELQAI
60 70 80 90 100
PNVTLFQGPL LNNVPLMDTL FEGAHLAFIN TTSQAGDEIA IGKDLADAAK
110 120 130 140 150
RAGTIQHYIY SSMPDHSLYG PWPAVPMWAP KFTVENYVRQ LGLPSTFVYA
160 170 180 190 200
GIYNNNFTSL PYPLFQMELM PDGTFEWHAP FDPDIPLPWL DAEHDVGPAL
210 220 230 240 250
LQIFKDGPQK WNGHRIALTF ETLSPVQVCA AFSRALNRRV TYVQVPKVEI
260 270 280 290 300
KVNIPVGYRE QLEAIEVVFG EHKAPYFPLP EFSRPAAGSP KGLGPANGKG
310 320 330 340 350
AGAGMMQGPG GVISQRVTDE ARKLWSGWRD MEEYAREVFP IEEEANGLDW

ML
Length:352
Mass (Da):38,796
Last modified:April 26, 2005 - v1
Checksum:i4E9982FFAE6F1F89
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti238 – 2381R → L in AAC39442 (PubMed:9537404).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041976 Genomic DNA. Translation: AAC39442.1.
AACD01000141 Genomic DNA. Translation: EAA59190.1.
BN001302 Genomic DNA. Translation: CBF74025.1.
RefSeqiXP_681437.1. XM_676345.1.

Genome annotation databases

EnsemblFungiiCADANIAT00004208; CADANIAP00004208; CADANIAG00004208.
EAA59190; EAA59190; AN8168.2.
GeneIDi2869210.
KEGGiani:AN8168.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041976 Genomic DNA. Translation: AAC39442.1.
AACD01000141 Genomic DNA. Translation: EAA59190.1.
BN001302 Genomic DNA. Translation: CBF74025.1.
RefSeqiXP_681437.1. XM_676345.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K6IX-ray1.80A1-352[»]
1K6JX-ray1.80A/B1-352[»]
1K6XX-ray1.50A1-352[»]
1TI7X-ray1.70A1-352[»]
1XGKX-ray1.40A1-352[»]
2VUSX-ray2.60A/B/C/D/E/F/G/H1-352[»]
2VUTX-ray2.30A/B/C/D/E/F/G/H1-352[»]
2VUUX-ray2.80A/B/C/D/E/F/G/H1-352[»]
ProteinModelPortaliQ5AU62.
SMRiQ5AU62. Positions 3-352.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00004208; CADANIAP00004208; CADANIAG00004208.
EAA59190; EAA59190; AN8168.2.
GeneIDi2869210.
KEGGiani:AN8168.2.

Organism-specific databases

EuPathDBiFungiDB:AN8168.

Phylogenomic databases

HOGENOMiHOG000160478.
InParanoidiQ5AU62.
OMAiANGLTWM.
OrthoDBiEOG75TMNQ.

Miscellaneous databases

EvolutionaryTraceiQ5AU62.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR008030. NmrA-like.
[Graphical view]
PfamiPF05368. NmrA. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the Aspergillus nidulans nmrA gene involved in nitrogen metabolite repression."
    Andrianopoulos A., Kourambas S., Sharp J.A., Davis M.A., Hynes M.J.
    J. Bacteriol. 180:1973-1977(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  4. "Expression, purification and crystallization of Aspergillus nidulans NmrA, a negative regulatory protein involved in nitrogen-metabolite repression."
    Nichols C.E., Cocklin S., Dodds A., Ren J., Lamb H., Hawkins A.R., Stammers D.K.
    Acta Crystallogr. D 57:1722-1725(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  5. "Transcriptional control of nmrA by the bZIP transcription factor MeaB reveals a new level of nitrogen regulation in Aspergillus nidulans."
    Wong K.H., Hynes M.J., Todd R.B., Davis M.A.
    Mol. Microbiol. 66:534-551(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY NITROGEN.
  6. "The structure of the negative transcriptional regulator NmrA reveals a structural superfamily which includes the short-chain dehydrogenase/reductases."
    Stammers D.K., Ren J., Leslie K., Nichols C.E., Lamb H.K., Cocklin S., Dodds A., Hawkins A.R.
    EMBO J. 20:6619-6626(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH NAD.
  7. "The negative transcriptional regulator NmrA discriminates between oxidized and reduced dinucleotides."
    Lamb H.K., Leslie K., Dodds A.L., Nutley M., Cooper A., Johnson C., Thompson P., Stammers D.K., Hawkins A.R.
    J. Biol. Chem. 278:32107-32114(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH NAD AND NADP, FUNCTION, INTERACTION WITH AREA.
  8. "Modulation of the ligand binding properties of the transcription repressor NmrA by GATA-containing DNA and site-directed mutagenesis."
    Lamb H.K., Ren J., Park A., Johnson C., Leslie K., Cocklin S., Thompson P., Mee C., Cooper A., Stammers D.K., Hawkins A.R.
    Protein Sci. 13:3127-3138(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF MUTANT GLY-12/GLY-18 APOPROTEIN, INTERACTION WITH AREA, FUNCTION, MUTAGENESIS OF ASN-12; THR-14; ALA-18; HIS-37; GLU-193; ASP-195; GLN-202; PHE-204; GLU-263 AND GLU-266.
  9. "Structural analysis of the recognition of the negative regulator NmrA and DNA by the zinc finger from the GATA-type transcription factor AreA."
    Kotaka M., Johnson C., Lamb H.K., Hawkins A.R., Ren J., Stammers D.K.
    J. Mol. Biol. 381:373-382(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEXES WITH NAD; NADP AND AREA, FUNCTION.

Entry informationi

Entry nameiNMRA_EMENI
AccessioniPrimary (citable) accession number: Q5AU62
Secondary accession number(s): C8V6Y1, O59919
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: April 26, 2005
Last modified: April 13, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

Lacks the conserved Tyr residue in position 127 in the active site triad of Ser-Tyr-Lys that is necessary for dehydrogenase activity, suggesting that it has no oxidoreductase activity.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.