ID A0A1Y0M5X4_9FLAO Unreviewed; 426 AA.
AC A0A1Y0M5X4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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 ORFNames=BTO04_02875 {ECO:0000313|EMBL:ARV05704.1};
OS Polaribacter sp. SA4-10.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=754397 {ECO:0000313|EMBL:ARV05704.1, ECO:0000313|Proteomes:UP000195822};
RN [1] {ECO:0000313|EMBL:ARV05704.1, ECO:0000313|Proteomes:UP000195822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA4-10 {ECO:0000313|EMBL:ARV05704.1,
RC ECO:0000313|Proteomes:UP000195822};
RA Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
RL Submitted (DEC-2016) 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 ---------------------------------------------------------------------------
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; CP019331; ARV05704.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0M5X4; -.
DR OrthoDB; 9801052at2; -.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000195822; Chromosome.
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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000195822}.
SQ SEQUENCE 426 AA; 46544 MW; 2E1D9997E5E3EF88 CRC64;
MAVLAKLTSQ EVIELENKHG AHNYHPLPVV LSKGEGVYVW DVEGKKYYDF LSAYSAVNQG
HCHPKIVDAM VNQAKTLTLT SRAFYNDMLG KYEKFATELF GFDKLLPMNT GAEAVETALK
LARKWAYEVK GIPENKAEII VCENNFHGRT TTIISFSNDP VARKNFGPYT KGFIKIEYDN
LQELQETLES SNNIAAFLVE PIQGEAGVYV PSEGYLATAK KMCEEYNVLF IADEVQTGIA
RTGRLLATCG NCSCENKNCE GTPEIKPDIL ILGKALSGGA YPVSAVLAND NVMNVIRPGN
HGSTFGGNPI AAAVAIAALE VVADDKLAIN ADNLGEIFRK ELSDFAEINS LVKSVRGKGL
LNAVLINDTE DSSTAWDICM KLRDNGLLAK PTHGNIIRFA PPLVINEAQL MDCISIIKNT
ITEFKK
//
