GenomeNet

Database: UniProt
Entry: A0A3D8GRW3_9BACI
LinkDB: A0A3D8GRW3_9BACI
Original site: A0A3D8GRW3_9BACI 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system