LOCUS NP_013127 418 aa linear PLN 17-DEC-2024
DEFINITION aspartate transaminase AAT2 [Saccharomyces cerevisiae S288C].
ACCESSION NP_013127
VERSION NP_013127.2
DBLINK BioProject: PRJNA128
DBSOURCE REFSEQ: accession NM_001181914.1
KEYWORDS RefSeq.
SOURCE Saccharomyces cerevisiae S288C
ORGANISM Saccharomyces cerevisiae S288C
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae;
Saccharomyces.
REFERENCE 1 (residues 1 to 418)
AUTHORS Engel,S.R., Wong,E.D., Nash,R.S., Aleksander,S., Alexander,M.,
Douglass,E., Karra,K., Miyasato,S.R., Simison,M., Skrzypek,M.S.,
Weng,S. and Cherry,J.M.
TITLE New data and collaborations at the Saccharomyces Genome Database:
updated reference genome, alleles, and the Alliance of Genome
Resources
JOURNAL Genetics 220 (4) (2022)
PUBMED 34897464
REFERENCE 2 (residues 1 to 418)
AUTHORS Johnston,M., Hillier,L., Riles,L., Albermann,K., Andre,B.,
Ansorge,W., Benes,V., Bruckner,M., Delius,H., Dubois,E.,
Dusterhoft,A., Entian,K.D., Floeth,M., Goffeau,A., Hebling,U.,
Heumann,K., Heuss-Neitzel,D., Hilbert,H., Hilger,F., Kleine,K.,
Kotter,P., Louis,E.J., Messenguy,F., Mewes,H.W., Hoheisel,J.D. et
al.
TITLE The nucleotide sequence of Saccharomyces cerevisiae chromosome XII
JOURNAL Nature 387 (6632 SUPPL), 87-90 (1997)
PUBMED 9169871
REFERENCE 3 (residues 1 to 418)
AUTHORS Goffeau,A., Barrell,B.G., Bussey,H., Davis,R.W., Dujon,B.,
Feldmann,H., Galibert,F., Hoheisel,J.D., Jacq,C., Johnston,M.,
Louis,E.J., Mewes,H.W., Murakami,Y., Philippsen,P., Tettelin,H. and
Oliver,S.G.
TITLE Life with 6000 genes
JOURNAL Science 274 (5287), 546 (1996)
PUBMED 8849441
REFERENCE 4 (residues 1 to 418)
CONSRTM NCBI Genome Project
TITLE Direct Submission
JOURNAL Submitted (17-DEC-2024) National Center for Biotechnology
Information, NIH, Bethesda, MD 20894, USA
REFERENCE 5 (residues 1 to 418)
CONSRTM Saccharomyces Genome Database
TITLE Direct Submission
JOURNAL Submitted (16-JAN-2015) Department of Genetics, Stanford
University, Stanford, CA, USA
REMARK Protein update by submitter
REFERENCE 6 (residues 1 to 418)
CONSRTM Saccharomyces Genome Database
TITLE Direct Submission
JOURNAL Submitted (06-FEB-2013) Department of Genetics, Stanford
University, Stanford, CA, USA
REMARK Protein update by submitter
REFERENCE 7 (residues 1 to 418)
CONSRTM Saccharomyces Genome Database
TITLE Direct Submission
JOURNAL Submitted (04-MAY-2012) Department of Genetics, Stanford
University, Stanford, CA, USA
REMARK Protein update by submitter
REFERENCE 8 (residues 1 to 418)
CONSRTM Saccharomyces Genome Database
TITLE Direct Submission
JOURNAL Submitted (31-MAR-2011) Department of Genetics, Stanford
University, Stanford, CA, USA
REMARK Sequence update by submitter
REFERENCE 9 (residues 1 to 418)
CONSRTM Saccharomyces Genome Database
TITLE Direct Submission
JOURNAL Submitted (14-DEC-2009) Department of Genetics, Stanford
University, Stanford, CA, USA
COMMENT REVIEWED REFSEQ: This record has been curated by SGD. The reference
sequence is identical to DAA09345.
On Oct 2, 2003 this sequence version replaced NP_013127.1.
##Genome-Annotation-Data-START##
Annotation Provider :: SGD
Annotation Status :: Full Annotation
Annotation Version :: R64-4-1
URL :: http://www.yeastgenome.org/
##Genome-Annotation-Data-END##
Method: conceptual translation.
FEATURES Location/Qualifiers
source 1..418
/organism="Saccharomyces cerevisiae S288C"
/strain="S288C"
/db_xref="taxon:559292"
/chromosome="XII"
Protein 1..418
/product="aspartate transaminase AAT2"
/EC_number="2.6.1.1"
/calculated_mol_wt=45927
Region 2..410
/region_name="AAT_I"
/note="Aspartate aminotransferase (AAT) superfamily (fold
type I) of pyridoxal phosphate (PLP)-dependent enzymes.
PLP combines with an alpha-amino acid to form a compound
called a Schiff base or aldimine intermediate, which
depending on the reaction, is the...; cl18945"
/db_xref="CDD:450240"
Site order(107..109,135,188,219,252,254..255,263)
/site_type="other"
/note="pyridoxal 5'-phosphate binding site [chemical
binding]"
/db_xref="CDD:99734"
Site order(110,145,212,261..263,303,306)
/site_type="other"
/note="homodimer interface [polypeptide binding]"
/db_xref="CDD:99734"
Site 255
/site_type="active"
/note="catalytic residue [active]"
/db_xref="CDD:99734"
CDS 1..418
/gene="AAT2"
/locus_tag="YLR027C"
/gene_synonym="ASP5"
/coded_by="NM_001181914.1:1..1257"
/experiment="EXISTENCE:direct assay:GO:0004069
L-aspartate:2-oxoglutarate aminotransferase activity
[PMID:1859361]"
/experiment="EXISTENCE:direct assay:GO:0005777 peroxisome
[PMID:9288922]"
/experiment="EXISTENCE:direct assay:GO:0005829 cytosol
[PMID:9288922]"
/experiment="EXISTENCE:direct assay:GO:0043023 ribosomal
large subunit binding [PMID:35621265]"
/experiment="EXISTENCE:mutant phenotype:GO:0004069
L-aspartate:2-oxoglutarate aminotransferase activity
[PMID:9288922]"
/experiment="EXISTENCE:mutant phenotype:GO:0005777
peroxisome [PMID:9288922]"
/experiment="EXISTENCE:mutant phenotype:GO:0006532
aspartate biosynthetic process
[PMID:15780654|PMID:9288922]"
/experiment="EXISTENCE:mutant phenotype:GO:0032938
negative regulation of translation in response to
oxidative stress [PMID:35621265]"
/note="Cytosolic aspartate aminotransferase involved in
the metabolism of nitrogen and amino acids such as
aspartate; localizes to and functions in peroxisomes in
oleate-grown cells; moonlighting role as a
ribosome-associated protein that modulates translation in
response to stress"
/db_xref="GeneID:850714"
/db_xref="SGD:S000004017"
ORIGIN
1 msatlfnnie llppdalfgi kqrygqdqra tkvdlgigay rddngkpwvl psvkaaekli
61 hndssynhey lgitglpslt snaakiifgt qsdafqedrv isvqslsgtg alhisakffs
121 kffpdklvyl skptwanhma ifenqglkta typywanetk sldlngflna iqkapegsif
181 vlhscahnpt gldptseqwv qivdaiaskn hialfdtayq gfatgdldkd ayavrlgvek
241 lstvspvfvc qsfaknagmy gervgcfhla ltkqaqnkti kpavtsqlak iirsevsnpp
301 aygakivakl letpelteqw hkdmvtmssr itkmrhalrd hlvklgtpgn wdhivnqcgm
361 fsftgltpqm vkrleethav ylvasgrasi aglnqgnvey vakaidevvr fytieakl
//