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Information on EC 6.1.1.11 - serine-tRNA ligase and Organism(s) Candida albicans and UniProt Accession Q9HGT6

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EC Tree
IUBMB Comments
This enzyme also recognizes tRNASec, the special tRNA for selenocysteine, and catalyses the formation of L-seryl-tRNASec, the substrate for EC 2.9.1.1, L-seryl-tRNASec selenium transferase.
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This record set is specific for:
Candida albicans
UNIPROT: Q9HGT6
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Word Map
The taxonomic range for the selected organisms is: Candida albicans
The enzyme appears in selected viruses and cellular organisms
Synonyms
serrs, seryl-trna synthetase, seryl trna synthetase, mtserrs, serrs2, mmbserrs, seryl-trna-synthetase, serzmo, methanogenic serrs, methanogenic-type serrs, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Seryl-tRNA synthetase
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62 kDa RNA-binding protein
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Serine transfer RNA synthetase
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Serine translase
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Serine--tRNA ligase
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SerRS
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SerRSmt
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SERSEC
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Seryl-transfer ribonucleate synthetase
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Seryl-transfer ribonucleic acid synthetase
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Seryl-transfer RNA synthetase
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Seryl-tRNA synthetase
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Synthetase, seryl-transfer ribonucleate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
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Aminoacylation
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PATHWAY SOURCE
PATHWAYS
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-, -, -
SYSTEMATIC NAME
IUBMB Comments
L-serine:tRNASer ligase (AMP-forming)
This enzyme also recognizes tRNASec, the special tRNA for selenocysteine, and catalyses the formation of L-seryl-tRNASec, the substrate for EC 2.9.1.1, L-seryl-tRNASec selenium transferase.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-48-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
two isozymes through poylmorphism at position 197, L197S
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
three-dimensional structure analysis, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified isozymes, sitting-drop vapour-diffusion method, 8-14 mg/ml protein in 50 mM Na HEPES, pH 7.6, 150 mM KCl, 10 mM MgCl2, and 8% v/v glycerol, is mixed with reservoir solution containing 100 mM Na MES pH 5.6-5.8, 3.2-3.4 M ammonium sulfate and 0-2% v/v glycerol, equilibration against 0.5 ml of reservoir solution. Binary complexes SerRS-SerSA and SerRS-ATP, SerRS_Ser197 with 15 mM 5'-O-[N-(l-seryl)sulfamoyl]adenosine or 10 mM ATP, are mixed with 100 mM Na MES pH 5.8-6.2, 3.3-3.4 M ammonium sulfate and 0-5% v/v glycerol as precipitant solution, 2-3 days, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement for analysis of crystal structures of unliganded SerRS and of its complexes with ATP and with a seryl-adenylate analogue
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged isozymes from Escherichia coli strain BL21 (DE3) by nickel affinity and anion exchange chromatography, followed by ultrafiltration and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
large-scale expression of His-tagged isozymes in Escherichia coli strain BL21 (DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rocha, R.; Barbosa Pereira, P.J.; Santos, M.A.; Macedo-Ribeiro, S.
Purification, crystallization and preliminary X-ray diffraction analysis of the seryl-tRNA synthetase from Candida albicans
Acta Crystallogr. Sect. F
67
153-156
2011
Candida albicans (Q9HGT6), Candida albicans
Manually annotated by BRENDA team