ID A0A3D8GRW3_9BACI Unreviewed; 398 AA.
AC A0A3D8GRW3;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Ornithine aminotransferase {ECO:0000256|ARBA:ARBA00012924, ECO:0000256|HAMAP-Rule:MF_01689};
DE Short=OAT {ECO:0000256|HAMAP-Rule:MF_01689};
DE EC=2.6.1.13 {ECO:0000256|ARBA:ARBA00012924, ECO:0000256|HAMAP-Rule:MF_01689};
DE AltName: Full=Ornithine--oxo-acid aminotransferase {ECO:0000256|ARBA:ARBA00030587, ECO:0000256|HAMAP-Rule:MF_01689};
GN Name=rocD {ECO:0000256|HAMAP-Rule:MF_01689};
GN ORFNames=DRW41_09345 {ECO:0000313|EMBL:RDU37220.1};
OS Neobacillus piezotolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=2259171 {ECO:0000313|EMBL:RDU37220.1, ECO:0000313|Proteomes:UP000257144};
RN [1] {ECO:0000313|EMBL:RDU37220.1, ECO:0000313|Proteomes:UP000257144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLB-04 {ECO:0000313|EMBL:RDU37220.1,
RC ECO:0000313|Proteomes:UP000257144};
RA Yu L., Tang X.;
RT "Bacillus sp. YLB-04 draft genome sequence.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of ornithine to glutamate
CC semialdehyde. {ECO:0000256|HAMAP-Rule:MF_01689}.
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|HAMAP-Rule:MF_01689};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_01689};
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|HAMAP-Rule:MF_01689}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01689}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. OAT subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_01689}.
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:RDU37220.1}.
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DR EMBL; QNQT01000003; RDU37220.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8GRW3; -.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000257144; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004587; F:ornithine aminotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
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 HAMAP; MF_01689; Ornith_aminotrans_3; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR010164; Orn_aminotrans.
DR InterPro; IPR034757; Ornith_aminotrans_bact.
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 Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01689};
KW Aminotransferase {ECO:0000256|HAMAP-Rule:MF_01689};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01689};
KW Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650, ECO:0000256|HAMAP-
KW Rule:MF_01689};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01689}; Reference proteome {ECO:0000313|Proteomes:UP000257144};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01689}.
FT MOD_RES 255
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01689"
SQ SEQUENCE 398 AA; 43877 MW; A8879C04332FF566 CRC64;
MAKTKDVIEQ TEKFGARNYH PLPIVISKAE GVWVEDPEGN KYMDMLSAYS AVNQGHRHPK
IIQALKDQAD RVTLTSRAFH NDQLGPWYEK ICKLTNKGMA LPMNTGAEAV ETAVKAARRW
AYFEKGVEEN QAEIIGCVGN FHGRTMTAVS LSSEEEYKKG FGPMLPGIKL VPYGDLNALK
EAITPNTAAF LIEPIQGEAG IIIPPEGYLK KAYELCKEHN VLFIADEIQA GLARSGKMFA
CEWEGFEPDM YILGKALGGG VFPISCVVAD KDILGVFNPG SHGSTFGGNP MACAVSIAAL
DVLIEEKLAD RSLELGEYFM GKLKGITNPR IKGVRGRGLF IGVELTEPAR KYCEQLKEEG
LLCKETHDTV IRFAPPLVIS KEELDWAIER IKKVLEKE
//