Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Binding sitei37NAD or NADP1 Publication1
Binding sitei80NAD or NADP1 Publication1
Binding sitei131NAD or NADP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 17NAD or NADP1 Publication6
Nucleotide bindingi153 – 156NAD or NADP1 Publication4

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

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)DescriptionActionsGraphical viewLength
Mutagenesisi12N → 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 Publication1
Mutagenesisi14T → 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 Publication1
Mutagenesisi18A → 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 Publication1
Mutagenesisi37H → 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 Publication1
Mutagenesisi193E → Q: No changes in the Kd for NAD and NADP and almost complete loss of affinity for areA; when associated with N-195. 1 Publication1
Mutagenesisi195D → N: No changes in the Kd for NAD and NADP and almost complete loss of affinity for areA; when associated with Q-193. 1 Publication1
Mutagenesisi202Q → 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 Publication1
Mutagenesisi204F → 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 Publication1
Mutagenesisi263E → Q: No changes in the Kd for NAD; NADP and areA; when associated with Q-266. 1 Publication1
Mutagenesisi266E → Q: No changes in the Kd for NAD; NADP and areA; when associated with Q-263. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003935681 – 352Nitrogen metabolite repression protein nmrAAdd BLAST352

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

1352
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 12Combined sources5
Helixi16 – 27Combined sources12
Beta strandi32 – 37Combined sources6
Helixi42 – 48Combined sources7
Beta strandi53 – 58Combined sources6
Helixi64 – 71Combined sources8
Beta strandi75 – 79Combined sources5
Helixi83 – 85Combined sources3
Helixi88 – 102Combined sources15
Beta strandi106 – 112Combined sources7
Helixi116 – 118Combined sources3
Beta strandi119 – 121Combined sources3
Turni126 – 128Combined sources3
Helixi129 – 139Combined sources11
Beta strandi141 – 143Combined sources3
Beta strandi145 – 150Combined sources6
Helixi154 – 156Combined sources3
Beta strandi158 – 161Combined sources4
Beta strandi166 – 169Combined sources4
Beta strandi175 – 181Combined sources7
Beta strandi183 – 185Combined sources3
Beta strandi187 – 190Combined sources4
Helixi192 – 206Combined sources15
Helixi208 – 211Combined sources4
Beta strandi215 – 218Combined sources4
Beta strandi220 – 223Combined sources4
Helixi225 – 236Combined sources12
Beta strandi240 – 244Combined sources5
Helixi256 – 269Combined sources14
Helixi280 – 282Combined sources3
Beta strandi283 – 285Combined sources3
Helixi319 – 324Combined sources6
Helixi331 – 337Combined sources7
Helixi339 – 345Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5AU62.

Family & Domainsi

Sequence similaritiesi

Belongs to the NmrA-type oxidoreductase family.Curated

Phylogenomic databases

HOGENOMiHOG000160478.
InParanoidiQ5AU62.
OMAiANGLTWM.
OrthoDBiEOG092C34CQ.

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)DescriptionActionsGraphical viewLength
Sequence conflicti238R → L in AAC39442 (PubMed:9537404).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

HOGENOMiHOG000160478.
InParanoidiQ5AU62.
OMAiANGLTWM.
OrthoDBiEOG092C34CQ.

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...

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: November 30, 2016
This is version 79 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.