1A110_ARATH
ID 1A110_ARATH Reviewed; 557 AA.
AC Q9LQ10;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Probable aminotransferase ACS10;
DE EC=2.6.1.-;
GN Name=ACS10; OrderedLocusNames=At1g62960; ORFNames=F16P17.11;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP LACK OF ACS ACTIVITY, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12968022; DOI=10.1074/jbc.m308297200;
RA Yamagami T., Tsuchisaka A., Yamada K., Haddon W.F., Harden L.A.,
RA Theologis A.;
RT "Biochemical diversity among the 1-amino-cyclopropane-1-carboxylate
RT synthase isozymes encoded by the Arabidopsis gene family.";
RL J. Biol. Chem. 278:49102-49112(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Probable aminotransferase. Does not have 1-aminocyclopropane-
CC 1-carboxylate synthase (ACS) activity, suggesting that it is not
CC involved in ethylene biosynthesis.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:12968022}.
CC -!- INDUCTION: By indole-3-acetic acid (IAA) and cycloheximide (CHX).
CC {ECO:0000269|PubMed:12968022}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- CAUTION: Contains a Gln instead of a Glu in position 176 and a Phe
CC residue instead of a Tyr in position 209; these residues being
CC essential in substrate recognition by ACS enzymes. {ECO:0000305}.
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DR EMBL; AC011000; AAF75807.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34027.1; -; Genomic_DNA.
DR EMBL; AF348575; AAK15546.1; -; mRNA.
DR EMBL; AY054691; AAK96882.1; -; mRNA.
DR EMBL; BT008906; AAP68345.1; -; mRNA.
DR PIR; D96654; D96654.
DR RefSeq; NP_564804.1; NM_104974.4.
DR AlphaFoldDB; Q9LQ10; -.
DR SMR; Q9LQ10; -.
DR BioGRID; 27819; 3.
DR STRING; 3702.AT1G62960.1; -.
DR iPTMnet; Q9LQ10; -.
DR PaxDb; Q9LQ10; -.
DR PRIDE; Q9LQ10; -.
DR ProteomicsDB; 245132; -.
DR EnsemblPlants; AT1G62960.1; AT1G62960.1; AT1G62960.
DR GeneID; 842598; -.
DR Gramene; AT1G62960.1; AT1G62960.1; AT1G62960.
DR KEGG; ath:AT1G62960; -.
DR Araport; AT1G62960; -.
DR TAIR; locus:2015509; AT1G62960.
DR eggNOG; KOG0256; Eukaryota.
DR HOGENOM; CLU_017584_1_0_1; -.
DR InParanoid; Q9LQ10; -.
DR OMA; AIISQHN; -.
DR OrthoDB; 1156861at2759; -.
DR PhylomeDB; Q9LQ10; -.
DR PRO; PR:Q9LQ10; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LQ10; baseline and differential.
DR Genevisible; Q9LQ10; AT.
DR GO; GO:0008793; F:aromatic-amino-acid:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..557
FT /note="Probable aminotransferase ACS10"
FT /id="PRO_0000123904"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 394
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 557 AA; 61016 MW; 78850961F7DB5236 CRC64;
MTRTEPNRSR SSNSDSDKNS GNVGGGRTTG MRVIVPLQGV VQGRGGLFLG SVIPCAFFYF
LQFYLKRNRK NDESDNSGEQ NSSASSSSSP NSGLPDPTRS QSAGHLTELT GLPRSLSRIL
LSPRNSGGAV SVSGRVNCVL KGGDSSPYYV GQKRVEDDPY DELGNPDGVI QLGLAQNNKL
SLDDWVLENP KEAISDGLSI SGIASYEPSD GLLELKMAVA GFMTEATKNS VTFDPSQLVL
TSGASSAIEI LSFCLADSGN AFLVPTPCSP GYDRDVKWRT GVDIIHVPCR SADNFNMSMV
VLDRAFYQAK KRGVRIRGII ISNPSNPMGS LLSRENLYAL LDFARERNIH IISNEIFAGS
VHGEEGEFVS MAEIVDTEEN IDRERVHIVY DLSKDLSFRG LRSAAIYSFN ESVLSASRKL
TTLSPVSSPT QHLLISAISN PKNVQRFVKT NRQRLQSIYT ELVEGLKELG IECTRSNGGF
YCWADMRGLI SSYSEKGEIE LWNKLLNIGK INVIPGSCCH CIEPGWFRIC FSNLSERDVP
VVMNRIRKVC ETCKSQN
