OAT_YEAST
ID OAT_YEAST Reviewed; 424 AA.
AC P07991; D6VZ72;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Ornithine aminotransferase {ECO:0000305};
DE Short=OTAse;
DE EC=2.6.1.13 {ECO:0000305|PubMed:3036506};
DE AltName: Full=Ornithine--oxo-acid aminotransferase;
GN Name=CAR2; Synonyms=CARGB; OrderedLocusNames=YLR438W; ORFNames=L9753.2;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2824201; DOI=10.1111/j.1432-1033.1987.tb13597.x;
RA Degols G.;
RT "Functional analysis of the regulatory region adjacent to the cargB gene of
RT Saccharomyces cerevisiae. Nucleotide sequence, gene fusion experiments and
RT cis-dominant regulatory mutation analysis.";
RL Eur. J. Biochem. 169:193-200(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55, FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, AND ACTIVITY REGULATION.
RC STRAIN=Sigma 1278B;
RX PubMed=3036506; DOI=10.1111/j.1432-1033.1987.tb11440.x;
RA Degols G., Jauniaux J.-C., Wiame J.M.;
RT "Molecular characterization of transposable-element-associated mutations
RT that lead to constitutive L-ornithine aminotransferase expression in
RT Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 165:289-296(1987).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-390, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Catalyzes the transamination of ornithine into L-glutamate
CC gamma-semialdehyde, the second step of arginine degradation.
CC {ECO:0000305|PubMed:3036506}.
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:0000305|PubMed:3036506};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13878;
CC Evidence={ECO:0000305|PubMed:3036506};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- ACTIVITY REGULATION: By arginine and urea.
CC {ECO:0000269|PubMed:3036506}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-ornithine: step 1/1.
CC {ECO:0000305|PubMed:3036506}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Present with 72000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; X06790; CAA29947.1; -; Genomic_DNA.
DR EMBL; U21094; AAB67514.1; -; Genomic_DNA.
DR EMBL; X05571; CAA29081.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09738.1; -; Genomic_DNA.
DR PIR; S59406; XNBYO.
DR RefSeq; NP_013542.1; NM_001182326.1.
DR AlphaFoldDB; P07991; -.
DR SMR; P07991; -.
DR BioGRID; 31696; 72.
DR DIP; DIP-1225N; -.
DR IntAct; P07991; 24.
DR MINT; P07991; -.
DR STRING; 4932.YLR438W; -.
DR iPTMnet; P07991; -.
DR MaxQB; P07991; -.
DR PaxDb; P07991; -.
DR PRIDE; P07991; -.
DR EnsemblFungi; YLR438W_mRNA; YLR438W; YLR438W.
DR GeneID; 851158; -.
DR KEGG; sce:YLR438W; -.
DR SGD; S000004430; CAR2.
DR VEuPathDB; FungiDB:YLR438W; -.
DR eggNOG; KOG1402; Eukaryota.
DR GeneTree; ENSGT00630000089895; -.
DR HOGENOM; CLU_016922_10_3_1; -.
DR InParanoid; P07991; -.
DR OMA; DVFPRFA; -.
DR BioCyc; MetaCyc:YLR438W-MON; -.
DR BioCyc; YEAST:YLR438W-MON; -.
DR Reactome; R-SCE-8964539; Glutamate and glutamine metabolism.
DR UniPathway; UPA00098; UER00358.
DR PRO; PR:P07991; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P07991; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0050155; F:ornithine(lysine) transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004587; F:ornithine-oxo-acid transaminase activity; IMP:SGD.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0006527; P:arginine catabolic process; IC:SGD.
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; IMP:SGD.
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 PANTHER; PTHR11986:SF18; PTHR11986:SF18; 1.
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 Aminotransferase; Cytoplasm; Isopeptide bond; Pyridoxal phosphate;
KW Reference proteome; Transferase; Ubl conjugation.
FT CHAIN 1..424
FT /note="Ornithine aminotransferase"
FT /id="PRO_0000120499"
FT MOD_RES 272
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CROSSLNK 390
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 8
FT /note="Missing (in Ref. 1; CAA29947 and 4; CAA29081)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="V -> L (in Ref. 1; CAA29947 and 4; CAA29081)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="F -> S (in Ref. 1; CAA29947)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="G -> R (in Ref. 1; CAA29947)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="H -> Q (in Ref. 1; CAA29947)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 46086 MW; A0B6BE492FC5C1B8 CRC64;
MSEATLSSKQ TIEWENKYSA HNYHPLPVVF HKAKGAHVWD PEGKLYLDFL SAYSAVNQGH
CHPHIIKALT EQAQTLTLSS RAFHNDVYAQ FAKFVTEFFG FETVLPMNTG AEAVETALKL
ARRWGYMKKN IPQDKAIILG AEGNFHGRTF GAISLSTDYE DSKLHFGPFV PNVASGHSVH
KIRYGHAEDF VPILESPEGK NVAAIILEPI QGEAGIVVPP ADYFPKVSAL CRKHNVLLIV
DEIQTGIGRT GELLCYDHYK AEAKPDIVLL GKALSGGVLP VSCVLSSHDI MSCFTPGSHG
STFGGNPLAS RVAIAALEVI RDEKLCQRAA QLGSSFIAQL KALQAKSNGI ISEVRGMGLL
TAIVIDPSKA NGKTAWDLCL LMKDHGLLAK PTHDHIIRLA PPLVISEEDL QTGVETIAKC
IDLL
