OAT_BOVIN
ID OAT_BOVIN Reviewed; 439 AA.
AC Q3ZCF5;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Ornithine aminotransferase, mitochondrial;
DE EC=2.6.1.13 {ECO:0000250|UniProtKB:P04181};
DE AltName: Full=Ornithine--oxo-acid aminotransferase;
DE Flags: Precursor;
GN Name=OAT;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible interconversion of L-ornithine and
CC 2-oxoglutarate to L-glutamate semialdehyde and L-glutamate.
CC {ECO:0000250|UniProtKB:P04181}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-ornithine = L-glutamate + L-glutamate 5-
CC semialdehyde; Xref=Rhea:RHEA:25160, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:46911, ChEBI:CHEBI:58066; EC=2.6.1.13;
CC Evidence={ECO:0000250|UniProtKB:P04181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25161;
CC Evidence={ECO:0000250|UniProtKB:P04181};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25162;
CC Evidence={ECO:0000250|UniProtKB:P04181};
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 {ECO:0000250|UniProtKB:P04181}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P04181}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P04181}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; BC102427; AAI02428.1; -; mRNA.
DR RefSeq; NP_001029412.1; NM_001034240.1.
DR AlphaFoldDB; Q3ZCF5; -.
DR SMR; Q3ZCF5; -.
DR STRING; 9913.ENSBTAP00000009097; -.
DR PaxDb; Q3ZCF5; -.
DR PeptideAtlas; Q3ZCF5; -.
DR PRIDE; Q3ZCF5; -.
DR GeneID; 505323; -.
DR KEGG; bta:505323; -.
DR CTD; 4942; -.
DR eggNOG; KOG1402; Eukaryota.
DR InParanoid; Q3ZCF5; -.
DR OrthoDB; 145181at2759; -.
DR BRENDA; 2.6.1.13; 908.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0050155; F:ornithine(lysine) transaminase activity; ISS:UniProtKB.
DR GO; GO:0004587; F:ornithine-oxo-acid transaminase 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; 3.40.640.10; -; 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 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 Acetylation; Aminotransferase; Mitochondrion; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 26..439
FT /note="Ornithine aminotransferase, mitochondrial"
FT /id="PRO_0000283043"
FT MOD_RES 49
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT MOD_RES 102
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT MOD_RES 107
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT MOD_RES 107
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT MOD_RES 292
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 362
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT MOD_RES 362
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT MOD_RES 386
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT MOD_RES 392
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT MOD_RES 405
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT MOD_RES 405
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P29758"
FT MOD_RES 421
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29758"
SQ SEQUENCE 439 AA; 48075 MW; 3A620B0CCDE3779E CRC64;
MLSKLARLQT VAGLGLGVHS SVASATSVAT KKTVQGPPSS DYIFERESKY GAHNYHPLPV
ALERGKGIYV WDVEGRKYFD FLSAYSAVNQ GHCHPKIVDA LKSQVDKLTL TSRAFYNNVL
GEYEEYVTKL FNYHKVLPMN TGVEAGETAC KLARKWGYTV KGIPKYKAKI VFAAGNFWGR
TLSAISSSTD PTSYDGFGPF MPGFEIIPYN DLPALERALQ DPNVAAFMVE PIQGEAGVVV
PDPGYLVGVR ELCTQHQVLF IADEIQTGLA RTGRWLAIDH ENVRPDIVLL GKALSGGLYP
VSAVLCDDEI MLTIKPGEHG STYGGNPLGC RVAIAALEVL EEENLAENAE KMGIILRNEL
MKLPSDVVTT VRGKGLLNAI VIRETKDCDA WKVCLRLRDN GLLAKPTHGD IIRFAPPLVI
KEDEILEAVE IINKTILSF
