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Database: UniProt
Entry: J9ISJ4_9SPIT
LinkDB: J9ISJ4_9SPIT
Original site: J9ISJ4_9SPIT 
ID   J9ISJ4_9SPIT            Unreviewed;       436 AA.
AC   J9ISJ4;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Ornithine aminotransferase {ECO:0000256|ARBA:ARBA00012924, ECO:0000256|RuleBase:RU365036};
DE            EC=2.6.1.13 {ECO:0000256|ARBA:ARBA00012924, ECO:0000256|RuleBase:RU365036};
GN   ORFNames=OXYTRI_19768 {ECO:0000313|EMBL:EJY82619.1};
OS   Oxytricha trifallax.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX   NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY82619.1};
RN   [1] {ECO:0000313|EMBL:EJY82619.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JRB310 {ECO:0000313|EMBL:EJY82619.1};
RX   PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA   Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA   Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA   Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA   Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA   Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT   "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT   with 16,000 Tiny Chromosomes.";
RL   PLoS Biol. 11:E1001473-E1001473(2013).
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:0000256|RuleBase:RU365036};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU365036};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-ornithine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004998, ECO:0000256|RuleBase:RU365036}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJY82619.1}.
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DR   EMBL; AMCR01005744; EJY82619.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9ISJ4; -.
DR   EnsemblProtists; EJY82619; EJY82619; OXYTRI_19768.
DR   OrthoDB; 884390at2759; -.
DR   UniPathway; UPA00098; UER00358.
DR   GO; GO:0004587; F:ornithine aminotransferase 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
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   NCBIfam; TIGR01885; Orn_aminotrans; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF18; ORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU365036,
KW   ECO:0000313|EMBL:EJY82619.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000256|RuleBase:RU365036, ECO:0000313|EMBL:EJY82619.1}.
SQ   SEQUENCE   436 AA;  48414 MW;  E669B4B0D7827FCF CRC64;
     MLSKTLAQRQ IKLAGSQMRA YATGFSNQAL IEKDLKYAAH NYKPLPVVLS RGQGIYVWDV
     EGKQYLDFLC GYSSNNQGHC HPKIIKELVE QAQKITLTSR AFYNDQMGLT AEYLTKLLGY
     DKMLPMNTGV EACETSVKLA RRWGYVKKGI PDDQAQVVMA KGNFWGRSIT ASGACDDPSR
     YHQFGPFTPG FPLVEYNNVE EVRKLFEADK NICAIMFEPI QGEGGVIVPD KNYLRNVKDL
     CKKHNVLMIL DEVQTGFGRT GKLMASDWEG VKPDILSVGK ALSGGTMPVS ASFCDDHIMM
     NIKPGDHGST YGGNPLGMAV ARVAIQTLIE ERMVENAFAM GDVFADQLSK IKSPLLKEQR
     GRGLFRAIEI VHDAKVKGDD LAYILMKLGL LTKASHDYSL RLAPALVIKE KEIMDACGII
     QDGFKQLEKL NKERSV
//
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