ID   A0A091MTT4_CARIC        Unreviewed;       439 AA.
AC   A0A091MTT4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Ornithine aminotransferase {ECO:0000256|ARBA:ARBA00012924, ECO:0000256|RuleBase:RU365036};
DE            EC=2.6.1.13 {ECO:0000256|ARBA:ARBA00012924, ECO:0000256|RuleBase:RU365036};
GN   ORFNames=N322_12736 {ECO:0000313|EMBL:KFP64890.1};
OS   Cariama cristata (Red-legged seriema).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Cariamiformes; Cariamidae; Cariama.
OX   NCBI_TaxID=54380 {ECO:0000313|EMBL:KFP64890.1, ECO:0000313|Proteomes:UP000054116};
RN   [1] {ECO:0000313|EMBL:KFP64890.1, ECO:0000313|Proteomes:UP000054116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N322 {ECO:0000313|EMBL:KFP64890.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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|ARBA:ARBA00004998, 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:RU003560}.
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DR   EMBL; KK516392; KFP64890.1; -; Genomic_DNA.
DR   RefSeq; XP_009698219.1; XM_009699917.1.
DR   AlphaFoldDB; A0A091MTT4; -.
DR   GeneID; 104161463; -.
DR   KEGG; ccri:104161463; -.
DR   CTD; 4942; -.
DR   OrthoDB; 884390at2759; -.
DR   UniPathway; UPA00098; UER00358.
DR   Proteomes; UP000054116; Unassembled WGS sequence.
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   CDD; cd00610; OAT_like; 1.
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; IPR049704; Aminotrans_3_PPA_site.
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   NCBIfam; TIGR01885; Orn_aminotrans; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF18; ORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU365036};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054116};
KW   Transferase {ECO:0000256|RuleBase:RU365036}.
SQ   SEQUENCE   439 AA;  48290 MW;  51277D15E87077DE CRC64;
     MFSKLTRSQS IAVLCRGVHA SLSSATSVAT KKTIQGPPSS DFIFEREAKY GAHNYHPLPV
     ALERGKGVYV WDVEGRKYFD FLSAYSAVNQ GHCHPKIVNA LKAQSEKLTL TSRAFYNDVL
     GEYEEFVTKM FNYNKVLPMN TGVEAGETAC KLARKWAYTV KGIPKYKAKV IFAAGNFWGR
     TMSAISSSTD PTSYDGFGPF MPGFEVIPYN DLPALERALQ DPNVAAFMVE PIQGEAGVVV
     PDKGYLTGVR DLCTKHNVLF IADEIQTGLA RTGKMLAVDH ENVRPDLVLL GKALSGGLYP
     VSAVLCDDEI MLTIKPGEHG STYGGNPLAC RVAMAALEVI EEEDLVKNAE IMGNILRNEL
     MKTPSDIVTS VRGKGLLNAI VIRETKDYDA WKVCLRLRDN GLLAKPTHGD IIRLAPPLVI
     KEDEIRECIE IIHKTILSF
//