ID A0A136IQJ0_9PEZI Unreviewed; 428 AA.
AC A0A136IQJ0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Ornithine aminotransferase {ECO:0000256|RuleBase:RU365036};
DE EC=2.6.1.13 {ECO:0000256|RuleBase:RU365036};
GN ORFNames=Micbo1qcDRAFT_185585 {ECO:0000313|EMBL:KXJ87191.1};
OS Microdochium bolleyi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ87191.1, ECO:0000313|Proteomes:UP000070501};
RN [1] {ECO:0000313|Proteomes:UP000070501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG DOE Joint Genome Institute;
RA David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA Barry K., Grigoriev I.V.;
RT "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT beachgrass.";
RL Submitted (FEB-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|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; KQ964263; KXJ87191.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136IQJ0; -.
DR STRING; 196109.A0A136IQJ0; -.
DR InParanoid; A0A136IQJ0; -.
DR OrthoDB; 2643465at2759; -.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000070501; 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 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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF18; ORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU365036};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000070501};
KW Transferase {ECO:0000256|RuleBase:RU365036, ECO:0000313|EMBL:KXJ87191.1}.
SQ SEQUENCE 428 AA; 46889 MW; 7D449A4AD8B3C522 CRC64;
MPASTLLRQG DNLSRKATEL LTLEDKYSAG GFGPLPGFVV SAKGSTLKVR PESRPLQPAN
YRSDPFQTNI AVHDHQWPIL AKTLCEKLGY DKVASMTSGA EAADAAVKIA RKWGIVRKGI
PAEELLVLGC SENYHGLSSG IWPLMTPGCG QQEYGITSVN NVNFDPETGK TLRYGHVEDF
EEVFEKYHGR IAAVMMEPIH GGLETFQEEI DFAAGVRQLC KKHNALFIAD EVRMGSGKTG
KFLCSDWLGS DNKPDMVVLG KSISGGAFPA SYVLGYNDTM TLVRPNQSAS TYAMSPAANA
STLAALCLYA DPNLLDRARV IQEKWREITS RWNYPFLRYC TGRGADLVIV LNEGEGGVTA
RRIARLAYQY GTLVYPQKPR IRCSVSLTIT DEELQKGMDN LSRAMADVSL YGDIPGDFHP
VDEVDAGF
//
