Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 6.1.1.11 - serine-tRNA ligase and Organism(s) Pyrococcus horikoshii and UniProt Accession O58441

for references in articles please use BRENDA:EC6.1.1.11
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Pyrococcus horikoshii
UNIPROT: O58441
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Pyrococcus horikoshii
The enzyme appears in selected viruses and cellular organisms
Synonyms
serrs, seryl-trna synthetase, seryl trna synthetase, mtserrs, serrs2, mmbserrs, seryl-trna-synthetase, serzmo, serrs1, methanogenic serrs, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Seryl-tRNA synthetase
-
62 kDa RNA-binding protein
-
-
-
-
Serine transfer RNA synthetase
-
-
-
-
Serine translase
-
-
-
-
Serine--tRNA ligase
-
-
-
-
SerRS
-
-
-
-
SerRSmt
-
-
-
-
SERSEC
-
-
-
-
Seryl-transfer ribonucleate synthetase
-
-
-
-
Seryl-transfer ribonucleic acid synthetase
-
-
-
-
Seryl-transfer RNA synthetase
-
-
-
-
Seryl-tRNA synthetase
-
-
-
-
Synthetase, seryl-transfer ribonucleate
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
-
-
-
-
Aminoacylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
show the reaction diagram
SerRS efficiently aminoacylates not only Pyrococcus horikoshii tRNA(Ser) but also bacterial tRNA(Ser)s from Thermus thermophilus and Escherichia coli
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of the SerRS from the archaeon Pyrococcus horikoshii bound with 5'-O-[N-(L-seryl)-sulfamoyl]-adenosine are solved at 2.6 A, with ATP at 2.8 A, and in the apo form at 3.0 A. SerRS recognizes the seryl and adenylate moieties in a manner similar to those of the bacterial and mitochondrial SerRSs from Thermus thermophilus and Bos taurus, respectively, but different from that of the unusual SerRS from the methanogenic archaeon Methanosarcina barkeri
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Itoh, Y.; Sekine, S.I.; Kuroishi, C.; Terada, T.; Shirouzu, M.; Kuramitsu, S.; Yokoyama, S.
Crystallographic and mutational studies of seryl-tRNA synthetase from the archaeon Pyrococcus horikoshii
RNA Biol.
5
169-177
2008
Pyrococcus horikoshii (O58441), Pyrococcus horikoshii
Manually annotated by BRENDA team