UniProtKB - Q5R4L6 (NIT2_PONAB)
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Protein
Omega-amidase NIT2
Gene
NIT2
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Functioni
Has a omega-amidase activity. The role of omega-amidase is to remove potentially toxic intermediates by converting alpha-ketoglutaramate and alpha-ketosuccinamate to biologically useful alpha-ketoglutarate and oxaloacetate, respectively.By similarity
Catalytic activityi
A monoamide of a dicarboxylate + H2O = a dicarboxylate + NH3.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 43 | Proton acceptorPROSITE-ProRule annotation | 1 | |
Active sitei | 112 | Proton donorPROSITE-ProRule annotation | 1 | |
Active sitei | 152 | NucleophilePROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- omega-amidase activity Source: UniProtKB-EC
GO - Biological processi
- nitrogen compound metabolic process Source: InterPro
Keywordsi
Molecular function | Hydrolase |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:NIT2 |
Organismi | Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
Taxonomic identifieri | 9601 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000320255 | 1 – 275 | Omega-amidase NIT2Add BLAST | 275 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 26 | PhosphoserineBy similarity | 1 | |
Modified residuei | 68 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 68 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 123 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 130 | N6-succinyllysineBy similarity | 1 |
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
PRIDEi | Q5R4L6. |
Interactioni
Subunit structurei
Homodimer.By similarity
Structurei
3D structure databases
ProteinModelPortali | Q5R4L6. |
SMRi | Q5R4L6. |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 4 – 247 | CN hydrolasePROSITE-ProRule annotationAdd BLAST | 244 |
Sequence similaritiesi
Phylogenomic databases
HOGENOMi | HOG000222700. |
HOVERGENi | HBG105126. |
InParanoidi | Q5R4L6. |
Family and domain databases
Gene3Di | 3.60.110.10. 1 hit. |
InterProi | View protein in InterPro IPR003010. C-N_Hydrolase. IPR036526. C-N_Hydrolase_sf. |
Pfami | View protein in Pfam PF00795. CN_hydrolase. 1 hit. |
SUPFAMi | SSF56317. SSF56317. 1 hit. |
PROSITEi | View protein in PROSITE PS50263. CN_HYDROLASE. 1 hit. |
i Sequence
Sequence statusi: Complete.
Q5R4L6-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MASFRLALIQ LQISSINSDN VTRACSFIRE AATQGAKIVS LPECFNSPYG
60 70 80 90 100
TKYFPEYAEK IPGESTQKLS EVAKECSIYL IGGSIPEEDA GKLYNTCAVF
110 120 130 140 150
GPDGTLLAKY RKIHLFDIDV PGKITFQESK TLSPGDSFCT FDTYCRVGLG
160 170 180 190 200
ICYDMRFAEL AQIYAQRGCQ LLVYPGAFNL TTGPAHWELL QRGRAVDNQV
210 220 230 240 250
YVATASPARD DKASYVAWGH STVVNPWGEV LAKAGTEEAI VYSDIDLKKL
260 270
AEIRQQIPVF RQKRSDLYAV EMKKP
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CR861230 Transcribed RNA. Translation: CAH93300.1. |
Similar proteinsi
Entry informationi
Entry namei | NIT2_PONAB | |
Accessioni | Q5R4L6Primary (citable) accession number: Q5R4L6 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 26, 2008 |
Last sequence update: | December 21, 2004 | |
Last modified: | October 25, 2017 | |
This is version 50 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |