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0GLSK_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameGLS
DescriptionGlutaminase kidney isoform, mitochondrial precursor (ec 3.5.1.2) (gls) (l-glutamine amidohydrolase) (k-glutaminase).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005739 mitochondrion (NAS)
0004359 glutaminase activity (NAS)
0006543 glutamine catabolism (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This family of enzymes deaminates glutamine to glutamate .
  IPR007043:Glutaminase
The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes. The few known examples from prokaryotes and viruses may be the result of horizontal gene transfers . The repeat has been found in proteins of diverse function such as transcriptional initiators.ell-cycle regulators.ytoskeletal.on transporters and signal transducers. The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures . Each repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90o angle. The repeats stack together to form an L-shaped structure .
  IPR002110:Ankyrin
This domain is present in the penicillin-binding protein family of beta-lactamases.hich constitute the most common bacterial resistance mechanism against beta-lactam antibiotics . Beta-lactamases appear to have evolved from DD-transpeptidases.hich are penicillin-binding proteins involved in cell wall biosynthesis.nd as such are one of the main targets of beta-lactam antibiotics. Both these proteins adopt a similar structure.onsisting of a cluster of helices and an alpha/beta sandwich. This beta-lactamase/transpeptidase fold is also present in other penicillin-binding proteins.s well as in esterase EstB .nd in D-aminopeptidase (N-terminal domain) . A probable glutaminase from Bacillus subtilis (YbgJ) may adopt a similar structure.nstead of the usual glutaminase fold.
  IPR012338:Penicillin-binding protein, transpeptidase fold
IPR007043:Glutaminase 
Evalue:-203.481491088867 
Location:244-530IPR002110:Ank 
Evalue:-6.408935546875 
Location:585-618IPR002110:ANK 
Evalue:0 
Location:12-25IPR002110:Ank 
Evalue:0.934498429298401 
Location:619-651
SequencesProtein: GLSK_HUMAN (669 aa)
mRNA: NM_014905
Local Annotation
Synapse Ontology
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
KO assignmentK01425
  Level 3 annotation:
    glutaminase
  Level 2 annotation:
    Nitrogen metabolism
    Glutamate metabolism
    D-Glutamine and D-glutamate metabolism
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 199 residues, 191453846-191454441Exon2: 34 residues, 191468122-191468219Exon3: 42 residues, 191468574-191468696Exon4: 45 residues, 191473534-191473664Exon5: 28 residues, 191474917-191474997Exon6: 56 residues, 191477974-191478138Exon7: 21 residues, 191483233-191483292Exon8: 13 residues, 191493994-191494027Exon9: 21 residues, 191494115-191494174Exon10: 24 residues, 191496887-191496954Exon11: 19 residues, 191497513-191497564Exon12: 61 residues, 191500276-191500453Exon13: 46 residues, 191503407-191503539Exon14: 33 residues, 191504515-191504608Exon15: 22 residues, 191526535-191526597Exon16: 27 residues, 191527554-191527631Exon17: 23 residues, 191527725-191527789Exon18: 905 residues, 191535800-191538510Exon19: 2 residues, -Jump to GLSK_HUMAN  
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