ID   OAT_KLULA               Reviewed;         437 AA.
AC   Q6CWC1;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Ornithine aminotransferase {ECO:0000303|PubMed:24912400};
DE            EC=2.6.1.13 {ECO:0000269|PubMed:24912400};
DE   AltName: Full=Ornithine--oxo-acid aminotransferase {ECO:0000250|UniProtKB:P07991};
GN   Name=CAR2 {ECO:0000303|PubMed:24912400}; OrderedLocusNames=KLLA0B05247g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
RN   [2]
RP   CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=24912400; DOI=10.1111/mmi.12666;
RA   Romagnoli G., Verhoeven M.D., Mans R., Fleury Rey Y., Bel-Rhlid R.,
RA   van den Broek M., Seifar R.M., Ten Pierick A., Thompson M., Muller V.,
RA   Wahl S.A., Pronk J.T., Daran J.M.;
RT   "An alternative, arginase-independent pathway for arginine metabolism in
RT   Kluyveromyces lactis involves guanidinobutyrase as a key enzyme.";
RL   Mol. Microbiol. 93:369-389(2014).
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:0000269|PubMed:24912400};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P07991};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-ornithine: step 1/1.
CC       {ECO:0000305|PubMed:24912400}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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; CR382122; CAH02161.1; -; Genomic_DNA.
DR   RefSeq; XP_451768.1; XM_451768.1.
DR   AlphaFoldDB; Q6CWC1; -.
DR   SMR; Q6CWC1; -.
DR   STRING; 28985.XP_451768.1; -.
DR   PRIDE; Q6CWC1; -.
DR   EnsemblFungi; CAH02161; CAH02161; KLLA0_B05247g.
DR   GeneID; 2896939; -.
DR   KEGG; kla:KLLA0_B05247g; -.
DR   eggNOG; KOG1402; Eukaryota.
DR   HOGENOM; CLU_016922_10_3_1; -.
DR   InParanoid; Q6CWC1; -.
DR   OMA; DVFPRFA; -.
DR   UniPathway; UPA00098; UER00358.
DR   Proteomes; UP000000598; Chromosome B.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0050155; F:ornithine(lysine) transaminase activity; IEA:UniProtKB-EC.
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:0010121; P:arginine catabolic process to proline via ornithine; IEA:EnsemblFungi.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006591; P:ornithine metabolic process; IEA:EnsemblFungi.
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; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..437
FT                   /note="Ornithine aminotransferase"
FT                   /id="PRO_0000432232"
SQ   SEQUENCE   437 AA;  47908 MW;  EB4AF6F8F83E6BD1 CRC64;
     MVVTAELNLS SAKTIEYEQE YSAHNYHPLP VVFSRASGAH VWDPEGKEYL DFLSAYSAVN
     QGHCHPHIIQ ALVDQASKLT LSSRAFSNDC FASFSKFVTE FFGYESVLPM NTGAEAVESA
     LKLARRWGYM VKKIQPNEAI ILGARGNFHG RTFGAISLST DEEDSRMNFG PFLENVTAKI
     PGGSDDEFIR YGEIDDYKRA FESHGDKICA VIVEPIQGEA GIVVPRADFL TDLQELCKKH
     QVLLICDEIQ TGIARTGKLL CYEHSPNCKP DIILLGKAIS GGVLPVSCVL SSREIMDCFT
     PGSHGSTYGG NPLASRVAIA ALEVVQNENL VERSARLGKF LQDELVKLQH ESNGVISEVR
     GKGLLTAIVI NPEKANGRTA WDLCLLMKDQ GVLAKPTHEH IIRLAPPLVI SEEDLLKGVD
     SIRVSLSKLP NVPKSHH