LOCUS NP_175988 314 aa linear PLN 20-OCT-2022
DEFINITION serine acetyltransferase 2;1 [Arabidopsis thaliana].
ACCESSION NP_175988
VERSION NP_175988.1
DBLINK BioProject: PRJNA116
BioSample: SAMN03081427
DBSOURCE REFSEQ: accession NM_104470.3
KEYWORDS RefSeq.
SOURCE Arabidopsis thaliana (thale cress)
ORGANISM Arabidopsis thaliana
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae;
Camelineae; Arabidopsis.
REFERENCE 1 (residues 1 to 314)
AUTHORS Theologis,A., Ecker,J.R., Palm,C.J., Federspiel,N.A., Kaul,S.,
White,O., Alonso,J., Altafi,H., Araujo,R., Bowman,C.L.,
Brooks,S.Y., Buehler,E., Chan,A., Chao,Q., Chen,H., Cheuk,R.F.,
Chin,C.W., Chung,M.K., Conn,L., Conway,A.B., Conway,A.R.,
Creasy,T.H., Dewar,K., Dunn,P., Etgu,P., Feldblyum,T.V., Feng,J.,
Fong,B., Fujii,C.Y., Gill,J.E., Goldsmith,A.D., Haas,B.,
Hansen,N.F., Hughes,B., Huizar,L., Hunter,J.L., Jenkins,J.,
Johnson-Hopson,C., Khan,S., Khaykin,E., Kim,C.J., Koo,H.L.,
Kremenetskaia,I., Kurtz,D.B., Kwan,A., Lam,B., Langin-Hooper,S.,
Lee,A., Lee,J.M., Lenz,C.A., Li,J.H., Li,Y., Lin,X., Liu,S.X.,
Liu,Z.A., Luros,J.S., Maiti,R., Marziali,A., Militscher,J.,
Miranda,M., Nguyen,M., Nierman,W.C., Osborne,B.I., Pai,G.,
Peterson,J., Pham,P.K., Rizzo,M., Rooney,T., Rowley,D., Sakano,H.,
Salzberg,S.L., Schwartz,J.R., Shinn,P., Southwick,A.M., Sun,H.,
Tallon,L.J., Tambunga,G., Toriumi,M.J., Town,C.D., Utterback,T.,
Van Aken,S., Vaysberg,M., Vysotskaia,V.S., Walker,M., Wu,D., Yu,G.,
Fraser,C.M., Venter,J.C. and Davis,R.W.
TITLE Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana
JOURNAL Nature 408 (6814), 816-820 (2000)
PUBMED 11130712
REFERENCE 2 (residues 1 to 314)
CONSRTM NCBI Genome Project
TITLE Direct Submission
JOURNAL Submitted (19-OCT-2022) National Center for Biotechnology
Information, NIH, Bethesda, MD 20894, USA
REFERENCE 3 (residues 1 to 314)
AUTHORS Krishnakumar,V., Cheng,C.-Y., Chan,A.P., Schobel,S., Kim,M.,
Ferlanti,E.S., Belyaeva,I., Rosen,B.D., Micklem,G., Miller,J.R.,
Vaughn,M. and Town,C.D.
TITLE Direct Submission
JOURNAL Submitted (18-JUL-2017) Plant Genomics, J. Craig Venter Institute,
9704 Medical Center Dr, Rockville, MD 20850, USA
REMARK Protein update by submitter
REFERENCE 4 (residues 1 to 314)
AUTHORS Krishnakumar,V., Cheng,C.-Y., Chan,A.P., Schobel,S., Kim,M.,
Ferlanti,E.S., Belyaeva,I., Rosen,B.D., Micklem,G., Miller,J.R.,
Vaughn,M. and Town,C.D.
TITLE Direct Submission
JOURNAL Submitted (17-MAY-2016) Plant Genomics, J. Craig Venter Institute,
9704 Medical Center Dr, Rockville, MD 20850, USA
REMARK Protein update by submitter
REFERENCE 5 (residues 1 to 314)
AUTHORS Swarbreck,D., Lamesch,P., Wilks,C. and Huala,E.
CONSRTM TAIR
TITLE Direct Submission
JOURNAL Submitted (18-FEB-2011) Department of Plant Biology, Carnegie
Institution, 260 Panama Street, Stanford, CA, USA
COMMENT REVIEWED REFSEQ: This record has been curated by TAIR and Araport.
The reference sequence is identical to AEE33320.
Method: conceptual translation.
FEATURES Location/Qualifiers
source 1..314
/organism="Arabidopsis thaliana"
/db_xref="taxon:3702"
/chromosome="1"
/ecotype="Columbia"
Protein 1..314
/product="serine acetyltransferase 2;1"
/calculated_mol_wt=34120
Region 1..314
/region_name="PLN02357"
/note="serine acetyltransferase"
/db_xref="CDD:215205"
Site order(180,182,197,231,261,264,266)
/site_type="other"
/note="trimer interface [polypeptide binding]"
/db_xref="CDD:100045"
Site order(196..197,216..217,223..224,231..232,243,258,
260..261,264,266,274,279)
/site_type="active"
/db_xref="CDD:100045"
Site order(196..197,223,231..232)
/site_type="other"
/note="substrate binding site [chemical binding]"
/db_xref="CDD:100045"
Site order(216..217,223..224,243,258,260..261,264,266,274,279)
/site_type="other"
/note="CoA binding site [chemical binding]"
/db_xref="CDD:100045"
CDS 1..314
/gene="SERAT2;1"
/locus_tag="AT1G55920"
/gene_synonym="ATSERAT2;1; F14J16.18; F14J16_18; SAT1;
SAT5; SERINE ACETYLTRANSFERASE; SERINE ACETYLTRANSFERASE
1; serine acetyltransferase 2;1; SERINE ACETYLTRANSFERASE
5"
/coded_by="NM_104470.3:263..1207"
/inference="Similar to RNA sequence,
EST:INSD:DR317416.1,INSD:DR317419.1,INSD:AI994235.1,
INSD:AU235623.1,INSD:DR317428.1,INSD:CB252675.1,
INSD:CB252671.1,INSD:EG495937.1,INSD:BP583119.1,
INSD:DR317423.1,INSD:BP800713.1,INSD:EH941888.1,
INSD:EL236680.1,INSD:BP844236.1,INSD:ES117412.1,
INSD:AU226359.1,INSD:DR317427.1,INSD:DR317417.1,
INSD:BP803278.1,INSD:EG495938.1,INSD:ES033294.1,
INSD:EL165255.1,INSD:AA067470.1,INSD:BP628180.1,
INSD:BP633752.1,INSD:T23000.1,INSD:DR317415.1,
INSD:DR317426.1,INSD:AV527893.1,INSD:DR317424.1,
INSD:BP609064.1,INSD:BP794320.1,INSD:AU238497.1,
INSD:DR317422.1,INSD:H36776.1,INSD:CB185723.2,
INSD:T22379.1,INSD:DR317418.1,INSD:DR317420.1,
INSD:EL004325.1,INSD:DR317421.1,INSD:T43238.1,
INSD:BP671912.1,INSD:H36645.1,INSD:AU229689.1,
INSD:BP583931.1,INSD:EH933482.1,INSD:DR317425.1,
INSD:EH831590.1,INSD:ES015877.1"
/inference="similar to RNA sequence,
mRNA:INSD:L42212.1,INSD:BT008309.1,INSD:AK227691.1"
/note="serine acetyltransferase 2;1 (SERAT2;1); FUNCTIONS
IN: serine O-acetyltransferase activity; INVOLVED IN:
cellular response to sulfate starvation, response to cold;
LOCATED IN: cytosol, chloroplast, nucleus; EXPRESSED IN:
22 plant structures; EXPRESSED DURING: 13 growth stages;
CONTAINS InterPro DOMAIN/s: Hexapeptide transferase,
conserved site (InterPro:IPR018357), Serine
O-acetyltransferase (InterPro:IPR005881), Trimeric
LpxA-like (InterPro:IPR011004), Serine acetyltransferase,
N-terminal (InterPro:IPR010493); BEST Arabidopsis thaliana
protein match is: serine acetyltransferase 2;2
(TAIR:AT3G13110.1); Has 24449 Blast hits to 24415 proteins
in 2638 species: Archae - 407; Bacteria - 18561; Metazoa -
8; Fungi - 223; Plants - 250; Viruses - 18; Other
Eukaryotes - 4982 (source: NCBI BLink)."
/db_xref="Araport:AT1G55920"
/db_xref="GeneID:842043"
/db_xref="TAIR:AT1G55920"
ORIGIN
1 matcidtcrt gntqdddsrf cciknffrpg fsvnrkihht qieddddvwi kmleeaksdv
61 kqepilsnyy yasitshrsl esalahilsv klsnlnlpsn tlfelfisvl eespeiiest
121 kqdliavker dpacisyvhc flgfkgflac qahriahtlw kqnrkivall iqnrvsesfa
181 vdihpgakig kgilldhatg vvigetavvg dnvsilhgvt lggtgkqsgd rhpkigdgvl
241 igagscilgn itigegakig sgsvvvkdvp arttavgnpa rliggkenpr khdkipcltm
301 dqtsyltews dyvi
//