ID E6WSA3_PSEUU Unreviewed; 498 AA.
AC E6WSA3;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:ADV27052.1};
GN OrderedLocusNames=Psesu_1204 {ECO:0000313|EMBL:ADV27052.1};
OS Pseudoxanthomonas suwonensis (strain 11-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=743721 {ECO:0000313|EMBL:ADV27052.1, ECO:0000313|Proteomes:UP000008632};
RN [1] {ECO:0000313|EMBL:ADV27052.1, ECO:0000313|Proteomes:UP000008632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11-1 {ECO:0000313|Proteomes:UP000008632};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Siebers A.K., Allgaier M., Thelen M.P.,
RA Hugenholtz P., Gladden J., Woyke T.;
RT "Complete sequence of Pseudoxanthomonas suwonensis 11-1.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC 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; CP002446; ADV27052.1; -; Genomic_DNA.
DR RefSeq; WP_013534881.1; NC_014924.1.
DR AlphaFoldDB; E6WSA3; -.
DR STRING; 743721.Psesu_1204; -.
DR KEGG; psu:Psesu_1204; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_042522_0_0_6; -.
DR OrthoDB; 6188639at2; -.
DR Proteomes; UP000008632; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43206:SF2; 4-AMINOBUTYRATE AMINOTRANSFERASE GABT; 1.
DR PANTHER; PTHR43206; AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ADV27052.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000008632};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADV27052.1}.
SQ SEQUENCE 498 AA; 53484 MW; 5710B1C13E548FAE CRC64;
MSVLAPLAPL RAHAGTRLTT GLDDAALERL AAGHPDLVAA IAAAGAEYTR QREDLADLLD
LDEEAQIAAL QEGFVNFYAD DCVTPYVALA ARGPWVVTLK GAVLYDAGGY GMLGFGHAPA
EALEAAGKPQ VMANIMTPSP SQRRFVKALR AEIGHSRGAC PFDRFMCLNS GSEAVGLACR
IVDINAKLQT DPGARHAGAT IKRLVVKGSF HGRTDRPALY SDSTRRTYRQ HLASYRNEDS
VLVVPPYDIA ALRKAFADAE ANGWFIEAVF LEPVMGEGDP GRAVPVDFYK AARELTRAHG
SLLLVDSIQA GLRAHGVLSL VDYPGFEGVE PPDMETYSKA LNAAQFPLSV LAVTADTAAL
YRKGVYGNTM TTNPRALDVA CATLGMLTPQ VRRNIRERGA QAVQKLEALK AELGGLITKV
QGTGLLFSCE LAPQFKCYGA GSTEEWLRMH GVNVIHGGEN SLRFTPHFAM DEDELDLLVS
MVGRALREGP RREQVAAA
//
