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Database: UniProt
Entry: A0A0V1N6W6_9BILA
LinkDB: A0A0V1N6W6_9BILA
Original site: A0A0V1N6W6_9BILA 
ID   A0A0V1N6W6_9BILA        Unreviewed;       820 AA.
AC   A0A0V1N6W6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=ornithine aminotransferase {ECO:0000256|ARBA:ARBA00012924};
DE            EC=2.6.1.13 {ECO:0000256|ARBA:ARBA00012924};
DE   AltName: Full=Ornithine--oxo-acid aminotransferase {ECO:0000256|ARBA:ARBA00030587};
DE   Flags: Fragment;
GN   Name=Oat {ECO:0000313|EMBL:KRZ79761.1};
GN   ORFNames=T10_1563 {ECO:0000313|EMBL:KRZ79761.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ79761.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ79761.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ79761.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-ornithine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004998}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954}.
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:KRZ79761.1}.
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DR   EMBL; JYDO01000005; KRZ79761.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1N6W6; -.
DR   STRING; 268474.A0A0V1N6W6; -.
DR   UniPathway; UPA00098; UER00358.
DR   Proteomes; UP000054843; Unassembled WGS sequence.
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; 2.120.10.30; TolB, C-terminal domain; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
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   InterPro; IPR012337; RNaseH-like_sf.
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   SUPFAM; SSF101898; NHL repeat; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:KRZ79761.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW   Transferase {ECO:0000313|EMBL:KRZ79761.1}.
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRZ79761.1"
FT   NON_TER         820
FT                   /evidence="ECO:0000313|EMBL:KRZ79761.1"
SQ   SEQUENCE   820 AA;  91325 MW;  09204E0E9B8D5FA2 CRC64;
     LEHQPSLPTT EPENSSSRTL NPTVIWSEPP PSIQESTVGE PPESDSAEDV LITPRTFNFE
     SWTEQSPWTE NVQSKAIGFI TSGRSGAVAV DPGKSRFMLH VKPTIVIEDQ ESVQLVMVNE
     LELDHFGKAS GMTLRNHILA VCSYTFGQIV LFEPETLKKL TELNCDGCTL FDLDIMSNGD
     LVSVDAKHEK VIKMRSTGER LAERHVHGAT RGVSVCMDDR IYVLVEGGPY IHLLDSFLNN
     LGTITFYKNQ SSKLDCRYLL CIENLLHISC DDAVYLLDVQ NGNVTSIQPT ENSVYGLGIG
     VDASDNVFVA KRGSSSVDVF KKDGQFLKTL NADRQFLCLG DAVAHGYKIM MDNFNIHLMM
     NNRTKLVGYK DEDVYTLLIR RSSDNTSMSA MSTEGEHTRS NFGLRATAKG KFFCEGCVFG
     SMTQKPHKEI IERRQSVPGE ILHANVCGPF IHPSVGGSRY FICFKDESSE YRMKGKGEIL
     RYLKIALAEI KQGIGCDVQR IRTYGGTEFV NKEFDKFLIE RGIVHEESSP YTPQCNEWLK
     ERTIHSLKRQ GEYEKFMTNL FGYDKLLLMN SGVEGCKSAL KLARRWAYDV KRVPENKAEV
     IFVEGNFWGR SLAAVSSSTD QESYGGFGPF MPGFKVIPYD DPRALEQVLN MNGNNVTAFM
     VEPIQGEAGV RVPKDGYLRK VAEICQRYNV LLVVHEVQTG LGRPGKRLCS DYENVRPDIL
     ILGKVLSGGC YPISAVLCDY SIMLNIKLGQ HGSTFGGNPL ACPLAMAAVR LVEEENLASN
     TFNMGQLFHQ QMHDLPSAIV KTVRGKGLLN AIEINNGYDV
//
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