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Database: UniProt
Entry: A0A151K0H2_9HYME
LinkDB: A0A151K0H2_9HYME
Original site: A0A151K0H2_9HYME 
ID   A0A151K0H2_9HYME        Unreviewed;       253 AA.
AC   A0A151K0H2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Ornithine aminotransferase {ECO:0000256|RuleBase:RU365036};
DE            EC=2.6.1.13 {ECO:0000256|RuleBase:RU365036};
GN   ORFNames=ALC56_02450 {ECO:0000313|EMBL:KYN43075.1};
OS   Trachymyrmex septentrionalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN43075.1, ECO:0000313|Proteomes:UP000078541};
RN   [1] {ECO:0000313|EMBL:KYN43075.1, ECO:0000313|Proteomes:UP000078541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN43075.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN43075.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex septentrionalis WGS genome.";
RL   Submitted (MAR-2016) 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; KQ981296; KYN43075.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151K0H2; -.
DR   STRING; 34720.A0A151K0H2; -.
DR   Proteomes; UP000078541; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
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   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU365036,
KW   ECO:0000313|EMBL:KYN43075.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU365036};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078541};
KW   Transferase {ECO:0000256|RuleBase:RU365036, ECO:0000313|EMBL:KYN43075.1}.
SQ   SEQUENCE   253 AA;  28513 MW;  7005FD6654D67774 CRC64;
     MPFTSQQVFD RESKYGAYNY HPLPVALCKD QGIFMWNVEG KRYFDFLSTY LAVNTHTKIH
     ISQNQVKIMF AESNFWGRTM SAVSSSIPNG YNGFGIDGAL QRTLVDPNVC AFMVEPIQGE
     ASVVVPKDGY LRGICELCWI ADKVRIAVDH ENAKPDILML GKALSGGFYL VFKILANDPI
     LLIIKGHLFR DELNKLPKEI ITLVRGKGLL NAIVINEKID AWDICVKLKD LIITEEQICE
     CADIIFKTIL TYT
//
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