ID A0A2A9MH37_9APIC Unreviewed; 441 AA.
AC A0A2A9MH37;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=BESB_052320 {ECO:0000313|EMBL:PFH35581.1};
OS Besnoitia besnoiti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Besnoitia.
OX NCBI_TaxID=94643 {ECO:0000313|EMBL:PFH35581.1, ECO:0000313|Proteomes:UP000224006};
RN [1] {ECO:0000313|EMBL:PFH35581.1, ECO:0000313|Proteomes:UP000224006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bb-Ger1 {ECO:0000313|EMBL:PFH35581.1,
RC ECO:0000313|Proteomes:UP000224006};
RA Schares G., Venepally P., Lorenzi H.A.;
RT "Genome sequencing of Besnoitia besnoiti strain Bb-Ger1.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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:PFH35581.1}.
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DR EMBL; NWUJ01000004; PFH35581.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9MH37; -.
DR STRING; 94643.A0A2A9MH37; -.
DR VEuPathDB; ToxoDB:BESB_052320; -.
DR OrthoDB; 884390at2759; -.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000224006; Chromosome iv.
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:PFH35581.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000224006};
KW Transferase {ECO:0000256|RuleBase:RU365036, ECO:0000313|EMBL:PFH35581.1}.
SQ SEQUENCE 441 AA; 48421 MW; AA0CEDFBE6D6E06D CRC64;
MAATADKVDL SAPNGGEWQM SIDTYRSGLN MKKEEDFFDC DRQYVCRNYA PVPVVISKGK
GARVWDINGN EYYDFLAGVS SLSQGHCHPR VVAALCRQAT RLTLTLRSFG NDITGPACRF
MAEMFGYDRV LLMNTGAEAG ESAVKIARKW AYEVKGVPHD SAKIILCKNN YWGRTIAACS
SSTTFECYNN FGPFTPGFTL IDYDDLDALE KALEDPHVAA FFVEPIQGEG GVNVPHPGYL
KRAHDLCKSK NVLLIADEIQ TGLCRTGRRL AVDHDGVHPD ILLLGKSLSA GVVPISAVMG
SAQVIDVLTP ATHGSTFGGN PLACAVAVEA LSVLRDENLA ERAERLGIKF RDRVTKELQG
RVPWIKEIRG KGLLNAIEVD SDLVNPNDIV MKLKENGILS KPTRVKVLRF IPPLVITDDE
HEDATAKIIK SFLAVDEERR K
//
