ID A0A0C2QWY7_9BACL Unreviewed; 397 AA.
AC A0A0C2QWY7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=KP78_38030 {ECO:0000313|EMBL:KIL42580.1};
OS Jeotgalibacillus soli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX NCBI_TaxID=889306 {ECO:0000313|EMBL:KIL42580.1, ECO:0000313|Proteomes:UP000031938};
RN [1] {ECO:0000313|EMBL:KIL42580.1, ECO:0000313|Proteomes:UP000031938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P9 {ECO:0000313|EMBL:KIL42580.1,
RC ECO:0000313|Proteomes:UP000031938};
RA Goh K.M., Chan K.-G., Yaakop A.S., Ee R., Gan H.M., Chan C.S.;
RT "Genome sequencing of Jeotgalibacillus soli.";
RL Submitted (JAN-2015) 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:KIL42580.1}.
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; JXRP01000022; KIL42580.1; -; Genomic_DNA.
DR RefSeq; WP_041090976.1; NZ_JXRP01000022.1.
DR AlphaFoldDB; A0A0C2QWY7; -.
DR STRING; 889306.KP78_38030; -.
DR PATRIC; fig|889306.3.peg.3819; -.
DR OrthoDB; 9807885at2; -.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000031938; 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; IPR049704; Aminotrans_3_PPA_site.
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 ECO:0000313|EMBL:KIL42580.1}; 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:UP000031938};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01689, ECO:0000313|EMBL:KIL42580.1}.
FT MOD_RES 255
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01689"
SQ SEQUENCE 397 AA; 43482 MW; A1F637A1C9FB6DB7 CRC64;
MTSSSSIIES TKQFGANNYH PLPVVISEAE GVWVKDPEGN KYMDMLSAYS AVNQGHRHPR
IIQALKDQAD KVTLTSRAFH NDQLGPWYEL ICKLSGKEMA LPMNTGAEAV ETAVKAARRW
GYDVKGIAPN KAEIIACNGN FHGRTMTAVS LSSEDEYKRG FGPMLPGVKR IPYGDIEALK
EAITPETAAF LFEPIQGEAG IVFPPAGFLK AARELCKENN ILFIADEIQT GLCRTGKMFA
CEWGNVDPDM YILGKALGGG VFPISCVVAN RDVLGVFNPG SHGSTFGGNP LACAVSIASL
NVLLDEKLAE RSLEMGAHFI RALQKIDNPI IKEIRGRGLF IGMELHEPAR KYCEALKQEG
LLCKETHDTV IRLAPPLVIT KDELDWAIDR IVRVLTR
//
