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
//