OAT_RAT
ID OAT_RAT Reviewed; 439 AA.
AC P04182; Q6LDF6; Q6LDF7;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 173.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=3840476; DOI=10.1016/s0021-9258(17)38826-9;
RA Mueckler M.M., Pitot H.C.;
RT "Sequence of the precursor to rat ornithine aminotransferase deduced from a
RT cDNA clone.";
RL J. Biol. Chem. 260:12993-12997(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3170546; DOI=10.1016/s0021-9258(18)68219-5;
RA Mitchell G.A., Looney J.E., Brody L.C., Steel G., Suchanek M.,
RA Engelhardt J.F., Willard H.F., Valle D.;
RT "Human ornithine-delta-aminotransferase. cDNA cloning and analysis of the
RT structural gene.";
RL J. Biol. Chem. 263:14288-14295(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1916291; DOI=10.1016/0378-1119(91)90251-6;
RA Shull J.D., Pennington K.L., George S.M., Kilibarda K.A.;
RT "The ornithine aminotransferase-encoding gene family of rat: cloning,
RT characterization, and evolutionary relationships between a single expressed
RT gene and three pseudogenes.";
RL Gene 104:203-209(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-97 AND 217-439.
RC STRAIN=Wistar Furth; TISSUE=Liver;
RX PubMed=1390894; DOI=10.1016/0167-4781(92)90016-s;
RA Shull J.D., Pennington K.L., Pitot H.C., Boryca V.S., Schulte B.L.;
RT "Isolation and characterization of the rat gene encoding ornithine
RT aminotransferase.";
RL Biochim. Biophys. Acta 1132:214-218(1992).
RN [6]
RP PROTEIN SEQUENCE OF 32-46; 275-292 AND 332-351, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 36-439.
RC TISSUE=Kidney;
RX PubMed=2229004; DOI=10.1093/oxfordjournals.jbchem.a123152;
RA Oyama R., Suzuki M., Matsuzawa T., Titani K.;
RT "Complete amino acid sequence of rat kidney ornithine aminotransferase:
RT identity with liver ornithine aminotransferase.";
RL J. Biochem. 108:133-138(1990).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, AND MASS
RP SPECTROMETRY.
RC STRAIN=Holtzman; TISSUE=Sperm;
RX PubMed=20966424; DOI=10.2164/jandrol.110.010967;
RA Suryawanshi A.R., Khan S.A., Gajbhiye R.K., Gurav M.Y., Khole V.V.;
RT "Differential proteomics leads to identification of domain specific
RT epididymal sperm proteins.";
RL J. Androl. 32:240-259(2011).
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 -!- 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 -!- TISSUE SPECIFICITY: Expressed in the head and flagellum of epididymal
CC sperm but not in testicular sperm (at protein level).
CC {ECO:0000269|PubMed:20966424}.
CC -!- MASS SPECTROMETRY: Mass=48302.04; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20966424};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; M11842; AAA41766.1; -; mRNA.
DR EMBL; BC061551; AAH61551.1; -; mRNA.
DR EMBL; M93296; AAA42060.1; -; Genomic_DNA.
DR EMBL; M93295; AAA42060.1; JOINED; Genomic_DNA.
DR EMBL; M93301; AAA42061.1; -; Genomic_DNA.
DR EMBL; M93297; AAA42061.1; JOINED; Genomic_DNA.
DR EMBL; M93298; AAA42061.1; JOINED; Genomic_DNA.
DR EMBL; M93299; AAA42061.1; JOINED; Genomic_DNA.
DR EMBL; M93300; AAA42061.1; JOINED; Genomic_DNA.
DR PIR; A00600; XNRTO.
DR RefSeq; NP_071966.1; NM_022521.3.
DR AlphaFoldDB; P04182; -.
DR SMR; P04182; -.
DR BioGRID; 249025; 1.
DR IntAct; P04182; 1.
DR STRING; 10116.ENSRNOP00000022628; -.
DR iPTMnet; P04182; -.
DR PhosphoSitePlus; P04182; -.
DR jPOST; P04182; -.
DR PaxDb; P04182; -.
DR PRIDE; P04182; -.
DR Ensembl; ENSRNOT00000022628; ENSRNOP00000022628; ENSRNOG00000016807.
DR GeneID; 64313; -.
DR KEGG; rno:64313; -.
DR UCSC; RGD:621724; rat.
DR CTD; 4942; -.
DR RGD; 621724; Oat.
DR eggNOG; KOG1402; Eukaryota.
DR GeneTree; ENSGT00630000089895; -.
DR HOGENOM; CLU_016922_10_3_1; -.
DR InParanoid; P04182; -.
DR OMA; DVFPRFA; -.
DR OrthoDB; 145181at2759; -.
DR PhylomeDB; P04182; -.
DR TreeFam; TF105720; -.
DR BRENDA; 2.6.1.13; 5301.
DR Reactome; R-RNO-8964539; Glutamate and glutamine metabolism.
DR SABIO-RK; P04182; -.
DR UniPathway; UPA00098; UER00358.
DR PRO; PR:P04182; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000016807; Expressed in jejunum and 20 other tissues.
DR Genevisible; P04182; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; TAS:RGD.
DR GO; GO:0050155; F:ornithine(lysine) transaminase activity; ISS:UniProtKB.
DR GO; GO:0004587; F:ornithine-oxo-acid transaminase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0019544; P:arginine catabolic process to glutamate; IBA:GO_Central.
DR GO; GO:0010121; P:arginine catabolic process to proline via ornithine; IBA:GO_Central.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006591; P:ornithine metabolic process; TAS:RGD.
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 1: Evidence at protein level;
KW Acetylation; Aminotransferase; Direct protein sequencing; Mitochondrion;
KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2229004"
FT CHAIN 36..439
FT /note="Ornithine aminotransferase, mitochondrial"
FT /id="PRO_0000001265"
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; 48333 MW; 254E5F541B92D461 CRC64;
MLSKLASLQT VAALRRGLRT SVASATSVAT KKTEQGPPSS EYIFERESKY GAHNYHPLPV
ALERGKGIYM WDVEGRQYFD FLSAYGAVSQ GHCHPKIIEA MKSQVDKLTL TSRAFYNNVL
GEYEEYITKL FNYNKVLPMN TGVEAGETAC KLARRWGYTV KGIQKYKAKI VFAVGNFWGR
TLSAVSSSTD PTSYDGFGPF MPGFETIPYN DLPALERALQ DPNVAAFMVE PIQGEAGVIV
PDPGYLTGVR ELCTRHQVLF IADEIQTGLA RTGRWLAVDH ENVRPDIVLL GKALSGGLYP
VSAVLCDDDI MLTIKPGEHG STYGGNPLGC RIAIAALEVL EEEHLAENAD KMGAILRKEL
MKLPSDVVTA VRGKGLLNAI VIRETKDCDA WKVCLRLRDN GLLAKPTHGD IIRLAPPLVI
KEDEIRESVE IINKTILSF
