ID A0A0W8IA87_9MICO Unreviewed; 409 AA.
AC A0A0W8IA87;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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:KUG56849.1};
GN ORFNames=AVL62_12005 {ECO:0000313|EMBL:KUG56849.1};
OS Serinicoccus chungangensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Serinicoccus.
OX NCBI_TaxID=767452 {ECO:0000313|EMBL:KUG56849.1, ECO:0000313|Proteomes:UP000054837};
RN [1] {ECO:0000313|EMBL:KUG56849.1, ECO:0000313|Proteomes:UP000054837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD08_5 {ECO:0000313|EMBL:KUG56849.1,
RC ECO:0000313|Proteomes:UP000054837};
RA Chander A.M., Kaur G., Nair G.R., Dhawan D.K., Kochhar R.K., Mayilraj S.,
RA Bhadada S.K.;
RT "Serinicoccus chungangenesis strain CD08_5 genome sequencing and
RT assembly.";
RL Submitted (DEC-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:KUG56849.1}.
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DR EMBL; LQBL01000011; KUG56849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W8IA87; -.
DR STRING; 767452.AVL62_12005; -.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000054837; 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; 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:KUG56849.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000054837};
KW Transferase {ECO:0000313|EMBL:KUG56849.1}.
SQ SEQUENCE 409 AA; 43143 MW; 9B3EE58B47C2D431 CRC64;
MTSMTELSTN QAYIDLEDQV AAHNYSPLPV VVGHAEGIHV TDVEGRTYID ALSGYSALNF
GHRHPGLVQA AKDQLDRSTL TSRAFHNDQL GPFCEALARL VGKDMILPMN TGAEAVETAL
KIARKWAYQV KGVPEGQAEI IVMDGNFHGR TTTIISFSDD PEAHDHYGPY TPGFVAVPYG
DLAAVEAAIT DNTAAVLVEP IQGEQGVMIP AEGYLPGLRE LCTRTNVLMI ADEIQSGLGR
TGTSLACEYE GVEADMYTLG KALGGGIVPV SAVAADAEVM NVITPGTHGS TFGGNPLAAA
VGKAVVDLLA TGEHQAHAKE LESVFAEELG QLVGQGAERV RVRGLWAGID IDPELMTGKE
ACKALAKKGV LAKDTHGSTI RLAPPLTITE DELRQITDAL AAVLAEARG
//
