UniProt: A0A091EQI5

Database: UniProt
Entry: A0A091EQI5_CORBR

LinkDB:  A0A091EQI5_CORBR 
Original site:  A0A091EQI5_CORBR

All links

Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (6)   
   Pfam (1)   
   PROSITE (1)   
All databases (16)   

Download RDF

ID   A0A091EQI5_CORBR        Unreviewed;       439 AA.
AC   A0A091EQI5;
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=N302_12081 {ECO:0000313|EMBL:KFO58867.1};
OS   Corvus brachyrhynchos (American crow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC   Corvus.
OX   NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO58867.1, ECO:0000313|Proteomes:UP000052976};
RN   [1] {ECO:0000313|EMBL:KFO58867.1, ECO:0000313|Proteomes:UP000052976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO58867.1};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KK718883; KFO58867.1; -; Genomic_DNA.
DR   RefSeq; XP_008631558.1; XM_008633336.2.
DR   AlphaFoldDB; A0A091EQI5; -.
DR   STRING; 85066.A0A091EQI5; -.
DR   GeneID; 103615316; -.
DR   KEGG; cbrc:103615316; -.
DR   CTD; 4942; -.
DR   OrthoDB; 884390at2759; -.
DR   UniPathway; UPA00098; UER00358.
DR   Proteomes; UP000052976; 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:UP000052976};
KW   Transferase {ECO:0000256|RuleBase:RU365036}.
SQ   SEQUENCE   439 AA;  48226 MW;  5631040114763BCA CRC64;
     MLSKLTRSQN LAVLCRGLHS SLSSATSVAP KKTIQGPPSS DFIFEREAKY GAHNYHPLPV
     ALERGKGVYV WDVEGRKYFD FLSAYSAVNQ GHCHPKIVDA LKAQSEKLAL TSRAFYNDVL
     GEYEELVTKM FNYNKVLPMN TGVEAGETAC KLARKWAYTV KGIPKYKAKI IFAAGNFWGR
     TMSAISSSTD PSSYDGFGPF MPGFELIPYN DLPALERALQ DPNVAAFMVE PIQGEAGVIV
     PDKGYLTGVR ELCTKHNVLF IADEIQTGLA RTGKMLAVDH ENVRPDIILL GKALSGGLYP
     VSAVLCDDEV MLTIKPGEHG STYGGNPLAC RVAMAALEVI EEENLAKNAE IMGNLLRNEL
     MKTPSNIVTA VRGKGLLNAI VIRETKDYDA WKVCLRLRDN GLLAKPTHGD IIRLAPPLVI
     KEDEIRESIE IIHKTILSF
//

DBGET integrated database retrieval system