OAT_ORYSJ
ID OAT_ORYSJ Reviewed; 473 AA.
AC Q10G56; A0A0N7KHQ2; Q60DP3;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Ornithine aminotransferase, mitochondrial;
DE EC=2.6.1.13;
DE AltName: Full=Ornithine delta-aminotransferase;
DE AltName: Full=Ornithine--oxo-acid aminotransferase;
DE Flags: Precursor;
GN Name=OAT; OrderedLocusNames=Os03g0643300, LOC_Os03g44150;
GN ORFNames=OSJNBa0038E17.15;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=23116672; DOI=10.1016/j.plantsci.2012.09.002;
RA You J., Hu H., Xiong L.;
RT "An ornithine delta-aminotransferase gene OsOAT confers drought and
RT oxidative stress tolerance in rice.";
RL Plant Sci. 197:59-69(2012).
CC -!- FUNCTION: Confers drought and oxidative stress tolerance mainly through
CC enhancing ROS-scavenging capacity and Pro pre-accumulation.
CC {ECO:0000269|PubMed:23116672}.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-ornithine: step 1/1.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- INDUCTION: Up-regulated by SNAC2. Also induced by high-salinity, heat,
CC and submergence. Strongly induced by abscisic acid (ABA) and auxin
CC (IAA), and slightly induced by brassinosteroid (BR) and jasmonic acid
CC (JA). {ECO:0000269|PubMed:23116672}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAU90265.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC145383; AAU90265.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000009; ABF97848.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF12667.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS85449.1; -; Genomic_DNA.
DR EMBL; AK099445; BAG94132.1; -; mRNA.
DR RefSeq; XP_015630389.1; XM_015774903.1.
DR AlphaFoldDB; Q10G56; -.
DR SMR; Q10G56; -.
DR STRING; 4530.OS03T0643300-02; -.
DR PaxDb; Q10G56; -.
DR PRIDE; Q10G56; -.
DR EnsemblPlants; Os03t0643300-02; Os03t0643300-02; Os03g0643300.
DR GeneID; 4333554; -.
DR Gramene; Os03t0643300-02; Os03t0643300-02; Os03g0643300.
DR KEGG; osa:4333554; -.
DR eggNOG; KOG1402; Eukaryota.
DR HOGENOM; CLU_016922_10_3_1; -.
DR InParanoid; Q10G56; -.
DR OMA; DVFPRFA; -.
DR OrthoDB; 145181at2759; -.
DR PlantReactome; R-OSA-1119289; Arginine degradation.
DR PlantReactome; R-OSA-1119318; Proline biosynthesis V (from arginine).
DR PlantReactome; R-OSA-1119495; Citrulline biosynthesis.
DR PlantReactome; R-OSA-1119610; Biotin biosynthesis II.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q10G56; OS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0019544; P:arginine catabolic process to glutamate; IBA:GO_Central.
DR GO; GO:0010121; P:arginine catabolic process to proline via ornithine; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IEA:EnsemblPlants.
DR GO; GO:0042538; P:hyperosmotic salinity response; IEA:EnsemblPlants.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0051646; P:mitochondrion localization; IEA:EnsemblPlants.
DR GO; GO:0006593; P:ornithine catabolic process; IEA:EnsemblPlants.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009733; P:response to auxin; IEP:UniProtKB.
DR GO; GO:0009741; P:response to brassinosteroid; IEP:UniProtKB.
DR GO; GO:0009413; P:response to flooding; IEP:UniProtKB.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IMP:UniProtKB.
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 2: Evidence at transcript level;
KW Aminotransferase; Mitochondrion; Pyridoxal phosphate; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 33..473
FT /note="Ornithine aminotransferase, mitochondrial"
FT /id="PRO_0000421299"
FT MOD_RES 293
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 473 AA; 51442 MW; 16E42093718DC21F CRC64;
MAAALARRGG GGLARALARG RGMCSATAAE RAAGAALTSE ELMRMERERS AHNYHPIPVV
FSKGEGSHIL DPEGNKYIDF LSAYSAVNQG HCHPKVLRAL KEQAERLTLS SRAFYNDKFP
IFAEYLTSMF GYEMMLPMNT GAEGVETAIK LVRKWGYEKK KIPKNEALIV SCCGCFHGRT
LGVISMSCDN DATRGFGPLV PGHLKVDFGD TDGLEKIFKD HGERICGFLF EPIQGEAGVI
IPPDGYLKAV RDLCSRHNIL MIADEIQTGI ARTGKMLACD WENIRPDVVI LGKALGAGVV
PVSAVLADKD IMLCIKPGEH GSTFGGNPLA SAVAVASLKV VTDEGLVERA AKLGQEFRDQ
LQKVQQRFPQ IIREVRGRGL LNAVDLSNEA LSPASAYDIC IKLKERGVLA KPTHDTIIRL
APPLSISPEE LAEASKAFSD VLEHDLPQLQ KQIKKTESAA EKQSCDRCGR DLY
