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Database: UniProt
Entry: H6BDN8_LOLPR
LinkDB: H6BDN8_LOLPR
Original site: H6BDN8_LOLPR 
ID   H6BDN8_LOLPR            Unreviewed;       188 AA.
AC   H6BDN8;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Ornithine aminotransferase {ECO:0000256|RuleBase:RU365036};
DE            EC=2.6.1.13 {ECO:0000256|RuleBase:RU365036};
DE   Flags: Fragment;
OS   Lolium perenne (Perennial ryegrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Poodae; Poeae; Poeae Chloroplast Group 2 (Poeae type);
OC   Loliodinae; Loliinae; Lolium.
OX   NCBI_TaxID=4522 {ECO:0000313|EMBL:AFA36584.1};
RN   [1] {ECO:0000313|EMBL:AFA36584.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Li H., Hu T., Fu J.;
RT   "Identification of genes involved in salinity tolerance in Lolium
RT   perenne.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU365036};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU365036};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-ornithine: step 1/1.
CC       {ECO:0000256|RuleBase:RU365036}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU365036}.
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DR   EMBL; JF747455; AFA36584.1; -; mRNA.
DR   AlphaFoldDB; H6BDN8; -.
DR   UniPathway; UPA00098; UER00358.
DR   GO; GO:0004587; F:ornithine aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF18; ORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   2: Evidence at transcript level;
KW   Aminotransferase {ECO:0000256|RuleBase:RU365036,
KW   ECO:0000313|EMBL:AFA36584.1};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU365036};
KW   Transferase {ECO:0000256|RuleBase:RU365036, ECO:0000313|EMBL:AFA36584.1}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFA36584.1"
FT   NON_TER         188
FT                   /evidence="ECO:0000313|EMBL:AFA36584.1"
SQ   SEQUENCE   188 AA;  20841 MW;  66BAE74011F9F580 CRC64;
     LRALIEQAER LTLSSRAFYN DKSPVFAQYL TSMFGYDMML PMNTGAEGVE TAIKLARKWG
     YEKKKIPKDE ALIVSCCGCF HGRTLGVISM SCDNDATRGF GPLVPGHLKV DFGDITALEK
     IFKEHGDRIC GFLFEPIQGE AGVILPPDGY LKSVRDLCSL HNILMIDDEI QTGIARTGKM
     LACDWEDV
//
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