ID A0A0R3PYB6_ANGCS Unreviewed; 354 AA.
AC A0A0R3PYB6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 36.
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=ACOC_LOCUS11399 {ECO:0000313|EMBL:VDM62984.1};
OS Angiostrongylus costaricensis (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0001139801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ACOC_0001139801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM62984.1, ECO:0000313|Proteomes:UP000267027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Costa Rica {ECO:0000313|EMBL:VDM62984.1,
RC ECO:0000313|Proteomes:UP000267027};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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}.
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DR EMBL; UYYA01004685; VDM62984.1; -; Genomic_DNA.
DR STRING; 334426.A0A0R3PYB6; -.
DR WBParaSite; ACOC_0001139801-mRNA-1; ACOC_0001139801-mRNA-1; ACOC_0001139801.
DR OMA; RSAWDLC; -.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000050601; Unplaced.
DR Proteomes; UP000267027; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000267027};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|RuleBase:RU365036};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..354
FT /note="Ornithine aminotransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040566099"
FT TRANSMEM 331..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 354 AA; 38770 MW; 00DB10FF75A88E3A CRC64;
MMSYLILLAC MSKSSIEDWD ASARVFVWDV AGKRYFDFLA AYSAVNQGHC HPRIVAAAVN
QLQQLSLTSR AFFNDVLGEY EEFLVKKFKY EKVLPMNTGV EACDSAVKLA RRWAYDVKKV
PNNQAKVVFA NENFWGRSIA AVSASTDPES YGGFGPFVPM FEKIPYNDLK SLEKGISDPN
TAAFMVEPIQ GEAGVVVPDD GYLKGVAELC KKHNVLFIAD EVQSGLGRTG ELLAHYYEGV
RPDIVILGKA LSGGVYPASA VLCDDHIMLN IKPGQHGSTY GGNPVACRVA IEALKVIDDE
RLVENSAAMG KILMAKLKTL PKDVVSVVRG RGLFCAVVIN PSMIFIVLYF IAYS
//
