OAT_ARATH
ID OAT_ARATH Reviewed; 475 AA.
AC Q9FNK4;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Ornithine aminotransferase, mitochondrial {ECO:0000303|PubMed:9576796};
DE EC=2.6.1.13 {ECO:0000269|PubMed:9576796};
DE AltName: Full=Ornithine delta-aminotransferase {ECO:0000303|PubMed:9576796};
DE AltName: Full=Ornithine--oxo-acid aminotransferase {ECO:0000303|PubMed:9576796};
DE Flags: Precursor;
GN Name=DELTA-OAT {ECO:0000303|PubMed:9576796};
GN OrderedLocusNames=At5g46180 {ECO:0000312|Araport:AT5G46180};
GN ORFNames=MCL19.24 {ECO:0000312|EMBL:BAB08263.1};
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], BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC
RP ACTIVITY, PATHWAY, AND INDUCTION BY SALT.
RC STRAIN=cv. Columbia;
RX PubMed=9576796; DOI=10.1104/pp.117.1.263;
RA Roosens N.H., Thu T.T., Iskandar H.M., Jacobs M.;
RT "Isolation of the ornithine-delta-aminotransferase cDNA and effect of salt
RT stress on its expression in Arabidopsis thaliana.";
RL Plant Physiol. 117:263-271(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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;
RA Kim C.J., Chen H., Cheuk R., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF Clone.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18419821; DOI=10.1186/1471-2229-8-40;
RA Funck D., Stadelhofer B., Koch W.;
RT "Ornithine-delta-aminotransferase is essential for arginine catabolism but
RT not for proline biosynthesis.";
RL BMC Plant Biol. 8:40-40(2008).
RN [7]
RP INDUCTION.
RX PubMed=20545884; DOI=10.1111/j.1365-3040.2010.02188.x;
RA Sharma S., Verslues P.E.;
RT "Mechanisms independent of abscisic acid (ABA) or proline feedback have a
RT predominant role in transcriptional regulation of proline metabolism during
RT low water potential and stress recovery.";
RL Plant Cell Environ. 33:1838-1851(2010).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY AVIRULENT PATHOGEN.
RX PubMed=22321246; DOI=10.1111/j.1365-3040.2012.02492.x;
RA Senthil-Kumar M., Mysore K.S.;
RT "Ornithine-delta-aminotransferase and proline dehydrogenase genes play a
RT role in non-host disease resistance by regulating pyrroline-5-carboxylate
RT metabolism-induced hypersensitive response.";
RL Plant Cell Environ. 35:1329-1343(2012).
CC -!- FUNCTION: Mediates degradation of arginine for nitrogen recycling.
CC Plays a role in non-host disease resistance by regulating pyrroline-5-
CC carboxylate metabolism-induced hypersensitive response.
CC {ECO:0000269|PubMed:18419821, ECO:0000269|PubMed:22321246}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-oxocarboxylate + L-ornithine = an L-alpha-amino acid + L-
CC glutamate 5-semialdehyde; Xref=Rhea:RHEA:13877, ChEBI:CHEBI:35179,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:58066, ChEBI:CHEBI:59869; EC=2.6.1.13;
CC Evidence={ECO:0000269|PubMed:9576796};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q5SHH5};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=91 mM for L-ornithine {ECO:0000269|PubMed:9576796};
CC Vmax=28 umol/h/mg enzyme toward L-glutamate 5-semialdehyde
CC {ECO:0000269|PubMed:9576796};
CC Note=The activity was enhanced in young plants under salt-stress
CC conditions. {ECO:0000269|PubMed:9576796};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-ornithine: step 1/1.
CC {ECO:0000269|PubMed:9576796}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P22256}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:18419821}.
CC -!- INDUCTION: By salt stress in young plants. Up-regulated during low
CC water potential. Induced upon non-host pathogen infection.
CC {ECO:0000269|PubMed:20545884, ECO:0000269|PubMed:22321246,
CC ECO:0000269|PubMed:9576796}.
CC -!- DISRUPTION PHENOTYPE: Unable to use arginine or ornithine as nitrogen
CC source. Displays sensitivity against type II non-host pathogen
CC infection. {ECO:0000269|PubMed:18419821, ECO:0000269|PubMed:22321246}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AB006698; BAB08263.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95350.1; -; Genomic_DNA.
DR EMBL; BT023421; AAY56412.1; -; mRNA.
DR EMBL; BT029160; ABJ17095.1; -; mRNA.
DR RefSeq; NP_199430.1; NM_123987.4.
DR AlphaFoldDB; Q9FNK4; -.
DR SMR; Q9FNK4; -.
DR STRING; 3702.AT5G46180.1; -.
DR iPTMnet; Q9FNK4; -.
DR SwissPalm; Q9FNK4; -.
DR PaxDb; Q9FNK4; -.
DR PRIDE; Q9FNK4; -.
DR ProteomicsDB; 239074; -.
DR EnsemblPlants; AT5G46180.1; AT5G46180.1; AT5G46180.
DR GeneID; 834660; -.
DR Gramene; AT5G46180.1; AT5G46180.1; AT5G46180.
DR KEGG; ath:AT5G46180; -.
DR Araport; AT5G46180; -.
DR TAIR; locus:2161398; AT5G46180.
DR eggNOG; KOG1402; Eukaryota.
DR HOGENOM; CLU_016922_10_3_1; -.
DR InParanoid; Q9FNK4; -.
DR OMA; DVFPRFA; -.
DR OrthoDB; 145181at2759; -.
DR PhylomeDB; Q9FNK4; -.
DR BioCyc; ARA:AT5G46180-MON; -.
DR BioCyc; MetaCyc:AT5G46180-MON; -.
DR BRENDA; 2.6.1.13; 399.
DR UniPathway; UPA00098; UER00358.
DR PRO; PR:Q9FNK4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNK4; baseline and differential.
DR Genevisible; Q9FNK4; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0050155; F:ornithine(lysine) transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004587; F:ornithine-oxo-acid transaminase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0019544; P:arginine catabolic process to glutamate; IMP:TAIR.
DR GO; GO:0010121; P:arginine catabolic process to proline via ornithine; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IEP:UniProtKB.
DR GO; GO:0042538; P:hyperosmotic salinity response; IDA:TAIR.
DR GO; GO:0051646; P:mitochondrion localization; IDA:CACAO.
DR GO; GO:0006593; P:ornithine catabolic process; IDA:UniProtKB.
DR GO; GO:0009626; P:plant-type hypersensitive response; TAS:UniProtKB.
DR GO; GO:0006561; P:proline biosynthetic process; IDA:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEA:EnsemblPlants.
DR GO; GO:0009733; P:response to auxin; IEA:EnsemblPlants.
DR GO; GO:0009741; P:response to brassinosteroid; IEA:EnsemblPlants.
DR GO; GO:0009413; P:response to flooding; IEA:EnsemblPlants.
DR GO; GO:0009408; P:response to heat; IEA:EnsemblPlants.
DR GO; GO:0009753; P:response to jasmonic acid; IEA:EnsemblPlants.
DR GO; GO:0006979; P:response to oxidative stress; IEA:EnsemblPlants.
DR GO; GO:0009651; P:response to salt stress; IDA:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEA:EnsemblPlants.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR010164; Orn_aminotrans.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11986:SF18; PTHR11986:SF18; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01885; Orn_aminotrans; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Mitochondrion; Plant defense; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 17..475
FT /note="Ornithine aminotransferase, mitochondrial"
FT /id="PRO_0000421298"
FT REGION 23..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 142..143
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q5SHH5"
FT BINDING 177
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q5SHH5"
FT BINDING 180
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:Q5SHH5"
FT BINDING 265..268
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q5SHH5"
FT BINDING 323
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:Q5SHH5"
FT BINDING 324
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q5SHH5"
FT MOD_RES 294
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q5SHH5"
SQ SEQUENCE 475 AA; 52178 MW; A886C999AB0B68CC CRC64;
MAATTRRLLY YVSKRFSTAG VRRSYGGLPQ SNSKSPPSSS QRLMELESEF SAHNYHPVPV
VFSRANGSTI WDPEGKRYID FLAAYSAVNQ GHCHPKIMKA LQEQVEKLTL SSRAFYNDKF
PVFAERLTNM FGYDMVLPMN TGAEGVETAL KLARKWGHEK KNIPKDEAII VSCCGCFHGR
TLAIVSMSCD NDATRGFGPL LPGNLKVDFG DADSLEKIFK EKGDRIAGFL FEPIQGEAGV
IIPPDGYLKA VRELCTKYNV LMIADEVQSG LARSGKMLAC DWEEIRPDMV ILGKALGGGV
IPVSAVLADK DVMLHIKPGQ HGSTFGGNPL ASAVAMASLD VIVEEKLVER SASLGEELRI
QLNEIKKQFP KYIKEVRGRG LFNAIEFNSE SLSPVSAYDI CLSLKERGVL AKPTHNTIVR
LTPPLSISSD ELRDGSEALH DVLELDLPNL LKINSGKTPV SHITECDRCG RNLYA
