ARGD_ARATH
ID ARGD_ARATH Reviewed; 457 AA.
AC Q9M8M7; Q56ZU0; Q8LDM4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Acetylornithine aminotransferase, chloroplastic/mitochondrial;
DE Short=ACOAT;
DE EC=2.6.1.11;
DE AltName: Full=Acetylornithine transaminase;
DE Short=AOTA;
DE AltName: Full=Protein HOPW1-1-INTERACTING 1;
DE Flags: Precursor;
GN Name=WIN1; OrderedLocusNames=At1g80600; ORFNames=T21F11.7;
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 [MRNA], FUNCTION, AND INTERACTION WITH PSEUDOMONAS
RP SYRINGAE MACULICOLA HOPW1-1.
RC STRAIN=cv. Wassilewskija;
RX PubMed=18266921; DOI=10.1111/j.1365-313x.2008.03439.x;
RA Lee M.W., Jelenska J., Greenberg J.T.;
RT "Arabidopsis proteins important for modulating defense responses to
RT Pseudomonas syringae that secrete HopW1-1.";
RL Plant J. 54:452-465(2008).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 401-457.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 42-54, ACETYLATION AT VAL-42, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-42, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER SER-41, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Involved in the biosynthesis of citrulline (By similarity).
CC Essential gene that modulates defense response to pathogenic bacteria,
CC conferring susceptibility and repressing salicylic acid (SA)
CC accumulation. {ECO:0000250, ECO:0000269|PubMed:18266921}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-
CC acetyl-L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:18049,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57805; EC=2.6.1.11;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 4/4.
CC -!- SUBUNIT: Interacts with the P.syringae pv. maculicola effector HopW1-1
CC (via C-terminus). {ECO:0000269|PubMed:18266921}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18431481}. Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; EU214908; ABW84224.1; -; mRNA.
DR EMBL; AC018849; AAF27117.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36426.1; -; Genomic_DNA.
DR EMBL; AY054594; AAK96785.1; -; mRNA.
DR EMBL; BT002584; AAO00944.1; -; mRNA.
DR EMBL; AY085912; AAM63124.1; -; mRNA.
DR EMBL; AK220871; BAD94250.1; -; mRNA.
DR PIR; B96838; B96838.
DR RefSeq; NP_178175.1; NM_106708.4.
DR AlphaFoldDB; Q9M8M7; -.
DR SMR; Q9M8M7; -.
DR BioGRID; 29617; 9.
DR STRING; 3702.AT1G80600.1; -.
DR iPTMnet; Q9M8M7; -.
DR PaxDb; Q9M8M7; -.
DR PRIDE; Q9M8M7; -.
DR ProteomicsDB; 246916; -.
DR EnsemblPlants; AT1G80600.1; AT1G80600.1; AT1G80600.
DR GeneID; 844399; -.
DR Gramene; AT1G80600.1; AT1G80600.1; AT1G80600.
DR KEGG; ath:AT1G80600; -.
DR Araport; AT1G80600; -.
DR TAIR; locus:2198948; AT1G80600.
DR eggNOG; KOG1401; Eukaryota.
DR HOGENOM; CLU_016922_10_1_1; -.
DR InParanoid; Q9M8M7; -.
DR OMA; FWGWQAH; -.
DR OrthoDB; 145181at2759; -.
DR PhylomeDB; Q9M8M7; -.
DR BioCyc; ARA:AT1G80600-MON; -.
DR UniPathway; UPA00068; UER00109.
DR PRO; PR:Q9M8M7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M8M7; baseline and differential.
DR Genevisible; Q9M8M7; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IMP:TAIR.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0006526; P:arginine biosynthetic process; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0080022; P:primary root development; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01107; ArgD_aminotrans_3; 1.
DR InterPro; IPR004636; AcOrn/SuccOrn_fam.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00707; argD; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Amino-acid biosynthesis; Aminotransferase;
KW Arginine biosynthesis; Chloroplast; Direct protein sequencing;
KW Mitochondrion; Plant defense; Plastid; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..41
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000269|PubMed:18431481,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 42..457
FT /note="Acetylornithine aminotransferase,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000403643"
FT MOD_RES 42
FT /note="N-acetylvaline; in Acetylornithine aminotransferase,
FT chloroplastic"
FT /evidence="ECO:0000269|PubMed:18431481,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 311
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 5
FT /note="S -> G (in Ref. 5; AAM63124)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="L -> F (in Ref. 5; AAM63124)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="H -> Y (in Ref. 5; AAM63124)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="S -> A (in Ref. 5; AAM63124)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 457 AA; 48827 MW; 081665877A10764F CRC64;
MASLSQITLP RAPSSEIGLL RRRLERPIIR TRIGFNGRIA SVLTNAGDQA VSVKASVSQK
VIEEEAKVIV GTYARAPVVL SSGKGCKLFD PEGKEYLDCA SGIAVNALGH GDPDWLRAVT
EQAGVLAHVS NVYYTIPQIE LAKRLVASSF ADRVFFCNSG TEANEAAIKF SRKFQRFTHP
EDKEVATGFI AFTNSFHGRT LGALALTSKE QYRTPFEPIM PGVTFLEYGN IQAATDLIRS
GKIAAVFVEP IQGEGGIYSA TKEFLQSLRS ACDAAGSLLV FDEVQCGLGR TGLMWAYEAF
GVTPDIMTVA KPLAGGLPIG AVLVTEKVAE TINYGDHGST FAGSPLVCSA AIAVMDKVSK
PSFLSSVSNK GRYFRDLLVK KLGGNSHVKE VRGEGLIIGV ELDVPASSLV DACRDSGLLI
LTAGKGNVVR IVPPLVISEE EIERAVEIMS QNLTALD
