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Database: UniProt
Entry: A0A1X2HJL3_SYNRA
LinkDB: A0A1X2HJL3_SYNRA
Original site: A0A1X2HJL3_SYNRA 
ID   A0A1X2HJL3_SYNRA        Unreviewed;       430 AA.
AC   A0A1X2HJL3;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=BCR43DRAFT_489029 {ECO:0000313|EMBL:ORY99283.1};
OS   Syncephalastrum racemosum (Filamentous fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Syncephalastraceae; Syncephalastrum.
OX   NCBI_TaxID=13706 {ECO:0000313|EMBL:ORY99283.1, ECO:0000313|Proteomes:UP000242180};
RN   [1] {ECO:0000313|EMBL:ORY99283.1, ECO:0000313|Proteomes:UP000242180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 2496 {ECO:0000313|EMBL:ORY99283.1,
RC   ECO:0000313|Proteomes:UP000242180};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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:ORY99283.1}.
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DR   EMBL; MCGN01000003; ORY99283.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2HJL3; -.
DR   STRING; 13706.A0A1X2HJL3; -.
DR   InParanoid; A0A1X2HJL3; -.
DR   OMA; RSAWDLC; -.
DR   OrthoDB; 884390at2759; -.
DR   UniPathway; UPA00098; UER00358.
DR   Proteomes; UP000242180; 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; 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; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000256|RuleBase:RU365036};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242180};
KW   Transferase {ECO:0000256|RuleBase:RU365036}.
SQ   SEQUENCE   430 AA;  47218 MW;  F0ECD9F47389E0E8 CRC64;
     MTQLSTEEYI QLEHDYSAHN YHPLPVVFAK AQGTRVWDPE GNEYLDFLSA YSAVNQGHCH
     PKIVKALCDQ AQILTLSSRA FYNNVFSSFS KYVTQYFGYD MVLPVNTGAE AVETAIKLAR
     RWGYVKKGIP DNEAIVLSCE NNFHGRTTGV ISMSTDKDSY GQFGPFLPLV GPKVNGSPLI
     RYNNADDLEA VLEKHGKHVA GFLVEPIQGE AGIMVPDEGY LKRCKALCEK HNVLFIADEI
     QTGLGRTGKK LCVEHDGVRP DVVLLGKALS GGVYPVSAVL ADKDVMLCIR PGEHGSTYGG
     NPLGCAAAIA ALEVIEDEKL SERAETLGEQ FRTQLRNIKS PLLQTVRGKG LLNAIVIDET
     QSDKTAWELC LLLKSRGLLA KPTHVNIIRL APPLVISEEE LTKAGQIIEQ ALNDIPKMTK
     EELKKLDISS
//
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