1A112_ARATH
ID 1A112_ARATH Reviewed; 495 AA.
AC Q8GYY0; Q9C5W4; Q9FLJ0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Probable aminotransferase ACS12;
DE EC=2.6.1.-;
GN Name=ACS12; OrderedLocusNames=At5g51690; ORFNames=K10D11.3, MIO24.18;
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 290-495.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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).
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. Expressed at low level in
CC leaves, stems, flowers and siliques. {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 Phe residue instead of a Tyr in position 151, the
CC Tyr residue being essential in substrate recognition by ACS enzymes.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11238.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC41994.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB010074; BAB11238.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96115.1; -; Genomic_DNA.
DR EMBL; AF336920; AAG54001.1; -; mRNA.
DR EMBL; BT000463; AAN17440.1; -; mRNA.
DR EMBL; BT002111; AAN72122.1; -; mRNA.
DR EMBL; AK117323; BAC41994.1; ALT_INIT; mRNA.
DR RefSeq; NP_199982.2; NM_124548.5.
DR AlphaFoldDB; Q8GYY0; -.
DR SMR; Q8GYY0; -.
DR STRING; 3702.AT5G51690.1; -.
DR PaxDb; Q8GYY0; -.
DR PRIDE; Q8GYY0; -.
DR ProteomicsDB; 244489; -.
DR EnsemblPlants; AT5G51690.1; AT5G51690.1; AT5G51690.
DR GeneID; 835243; -.
DR Gramene; AT5G51690.1; AT5G51690.1; AT5G51690.
DR KEGG; ath:AT5G51690; -.
DR Araport; AT5G51690; -.
DR TAIR; locus:2165306; AT5G51690.
DR eggNOG; KOG0256; Eukaryota.
DR HOGENOM; CLU_017584_1_0_1; -.
DR InParanoid; Q8GYY0; -.
DR OrthoDB; 1156861at2759; -.
DR PhylomeDB; Q8GYY0; -.
DR PRO; PR:Q8GYY0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GYY0; baseline and differential.
DR Genevisible; Q8GYY0; 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; IPR004838; NHTrfase_class1_PyrdxlP-BS.
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.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 2: Evidence at transcript level;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..495
FT /note="Probable aminotransferase ACS12"
FT /id="PRO_0000123906"
FT MOD_RES 334
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 495 AA; 55214 MW; 66C89DF8501044A2 CRC64;
MRLIVPLRGV IQGRGGLFVG SLIPCCLFYF LQLYLKRRRP PPSDPTDLPR TFSRTNLFSR
GNSIGRVRVS SRAVPVAKPS DSPYYIGLER VKTDPYDRIT NTDGIIQLGL AESTLCFDLL
QRWMSENLME SMMQSDDGEF DISSIAMYKP FEGLLELRVA FADFMSRIMG GNVSFDPSNM
VITAGGTPAI EVLAFCLADH GNAFLIPTPY YPGFDRDIKF RTGVELIPVH CRSSDNFTVT
VSALEQALNQ ARKRGSKVSG ILFSNPSNPV GNILSRETLC DILRFAQEKN IHVISDEIFA
GSVYGDKEFV SMAEIAGSGE FDKTRVHIIY GLSKDLSIPG FRAGVIYSFH EDVVNAAKKL
MRFSSVPVLV QRILISLLSD VRFIEGYMAA HRQRIRDKHI RFVEGLKQLG IPCAESGGGL
YCWVDMSSLL TSYSEKGELE LFEKLLTVAK INATPGTACY CIEPGWFRCC FTALADEDIP
VIMERIRQLA ESFRS
