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Database: UniProt
Entry: A0A0N0XVY8_9ACTN
LinkDB: A0A0N0XVY8_9ACTN
Original site: A0A0N0XVY8_9ACTN 
ID   A0A0N0XVY8_9ACTN        Unreviewed;       411 AA.
AC   A0A0N0XVY8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
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};
GN   Name=rocD {ECO:0000313|EMBL:KPC61157.1};
GN   ORFNames=ADL29_25600 {ECO:0000313|EMBL:KPC61157.1};
OS   Streptomyces chattanoogensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=66876 {ECO:0000313|EMBL:KPC61157.1, ECO:0000313|Proteomes:UP000037982};
RN   [1] {ECO:0000313|Proteomes:UP000037982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL ISP-5002 {ECO:0000313|Proteomes:UP000037982};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-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|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:KPC61157.1}.
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DR   EMBL; LGKG01000151; KPC61157.1; -; Genomic_DNA.
DR   RefSeq; WP_053925935.1; NZ_LGKG01000151.1.
DR   AlphaFoldDB; A0A0N0XVY8; -.
DR   PATRIC; fig|66876.3.peg.5615; -.
DR   UniPathway; UPA00098; UER00358.
DR   Proteomes; UP000037982; 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; 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:0000313|EMBL:KPC61157.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037982};
KW   Transferase {ECO:0000313|EMBL:KPC61157.1}.
SQ   SEQUENCE   411 AA;  43466 MW;  EC752F2CCC6FCE24 CRC64;
     MTAPARIARP GTPRSSAELI KSEAPVLAHN YHPLPVVIAR AEGVWVEDVE GRRYLDMLAG
     YSALNFGHRH PDLIEAAHRQ LDQLTLTSRA FHHDRLAGFA AGLAELTGLD MVLPMNTGAE
     AVESGVKVAR KWAYDVKGIP ADQATVIVAS GNFHGRTTTI ISFSDDDTAR AGFGPFTPGF
     RVVPYNDIPA LEAAIDSTTA AVLIEPIQGE AGVRIPDDGY LTAVRDLTRR ENCLLIADEI
     QSGLGRTGRT LAMDHESVTP DILLLGKALG GGIVPVSAVV ARREVMSVLG PGQHGSTFGG
     NPLAAAVGSA VIDLLATGEF QARAAELGKV LRAGLEDLST HGVTGFRTRG LWAGIDIDPS
     LGTGRTLCER LLQEGILVKD THGSTIRMAP PLTITREELE GALAGLRRAL A
//
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