OAT_MOUSE
ID OAT_MOUSE Reviewed; 439 AA.
AC P29758;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 171.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3HF; TISSUE=Liver;
RA Manenti G., Gariboldi M., Pierotti M.A., della Porta G., Dragani T.A.;
RL Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [3]
RP PROTEIN SEQUENCE OF 26-45.
RC TISSUE=Liver;
RX PubMed=1286668; DOI=10.1002/elps.11501301200;
RA Giometti C.S., Taylor J., Tollaksen S.L.;
RT "Mouse liver protein database: a catalog of proteins detected by two-
RT dimensional gel electrophoresis.";
RL Electrophoresis 13:970-991(1992).
RN [4]
RP PROTEIN SEQUENCE OF 170-180.
RC TISSUE=Brain;
RA Lubec G., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-102; LYS-107; LYS-362 AND
RP LYS-405, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-49; LYS-66; LYS-107; LYS-362;
RP LYS-386; LYS-392; LYS-405 AND LYS-421, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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 -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; X64837; CAA46049.1; -; mRNA.
DR EMBL; BC008119; AAH08119.1; -; mRNA.
DR CCDS; CCDS21923.1; -.
DR PIR; S19937; XNMSO.
DR RefSeq; NP_058674.1; NM_016978.2.
DR AlphaFoldDB; P29758; -.
DR SMR; P29758; -.
DR BioGRID; 201887; 8.
DR IntAct; P29758; 2.
DR STRING; 10090.ENSMUSP00000081544; -.
DR ChEMBL; CHEMBL1075297; -.
DR CarbonylDB; P29758; -.
DR iPTMnet; P29758; -.
DR PhosphoSitePlus; P29758; -.
DR SwissPalm; P29758; -.
DR REPRODUCTION-2DPAGE; IPI00129178; -.
DR REPRODUCTION-2DPAGE; P29758; -.
DR SWISS-2DPAGE; P29758; -.
DR EPD; P29758; -.
DR jPOST; P29758; -.
DR PaxDb; P29758; -.
DR PeptideAtlas; P29758; -.
DR PRIDE; P29758; -.
DR ProteomicsDB; 294263; -.
DR Antibodypedia; 32371; 256 antibodies from 32 providers.
DR DNASU; 18242; -.
DR Ensembl; ENSMUST00000084500; ENSMUSP00000081544; ENSMUSG00000030934.
DR GeneID; 18242; -.
DR KEGG; mmu:18242; -.
DR UCSC; uc009kcb.1; mouse.
DR CTD; 4942; -.
DR MGI; MGI:97394; Oat.
DR VEuPathDB; HostDB:ENSMUSG00000030934; -.
DR eggNOG; KOG1402; Eukaryota.
DR GeneTree; ENSGT00630000089895; -.
DR HOGENOM; CLU_016922_10_3_1; -.
DR InParanoid; P29758; -.
DR OMA; DVFPRFA; -.
DR OrthoDB; 145181at2759; -.
DR PhylomeDB; P29758; -.
DR TreeFam; TF105720; -.
DR BRENDA; 2.6.1.13; 3474.
DR Reactome; R-MMU-8964539; Glutamate and glutamine metabolism.
DR UniPathway; UPA00098; UER00358.
DR BioGRID-ORCS; 18242; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Oat; mouse.
DR PRO; PR:P29758; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P29758; protein.
DR Bgee; ENSMUSG00000030934; Expressed in migratory enteric neural crest cell and 264 other tissues.
DR ExpressionAtlas; P29758; baseline and differential.
DR Genevisible; P29758; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; 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 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..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1286668"
FT CHAIN 26..439
FT /note="Ornithine aminotransferase, mitochondrial"
FT /id="PRO_0000001264"
FT MOD_RES 49
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 102
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 107
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 107
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
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:0007744|PubMed:23576753"
FT MOD_RES 362
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 386
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 392
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 405
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 405
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 421
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
SQ SEQUENCE 439 AA; 48355 MW; 74299A63F6C48025 CRC64;
MLSKLASLQT IAALRRGVHT SVASATSVAT KKTEQGPPSS EYIFERESKY GAHNYHPLPV
ALERGKGIYM WDVEGRQYFD FLSAYGAVSQ GHCHPKIIDA MKSQVDKLTL TSRAFYNNVL
GEYEEYITKL FNYNKVLPMN TGVEAGETAC KLARRWGYTV KGIQKYKAKI VFADGNFWGR
TLSAISSSTD PTSYDGFGPF MPGFETIPYN DLPALERALQ DPNVAAFMVE PIQGEAGVIV
PDPGYLTGVR ELCTRHQVLF IADEIQTGLA RTGRWLAVDH ENVRPDMVLL GKALSGGLYP
VSAVLCDDEI MLTIKPGEHG STYGGNPLGC RIAIAALEVL EEENLAENAD KMGAILRKEL
MKLPSDVVTS VRGKGLLNAI VIRETKDCDA WKVCLRLRDN GLLAKPTHGD IIRLAPPLVI
KEDEIRESVE IINKTILSF
