ID Q1IFD8_PSEE4 Unreviewed; 448 AA.
AC Q1IFD8;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Beta-alanine--pyruvate transaminase {ECO:0000313|EMBL:CAK13616.1};
DE EC=2.6.1.18 {ECO:0000313|EMBL:CAK13616.1};
GN OrderedLocusNames=PSEEN0681 {ECO:0000313|EMBL:CAK13616.1};
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676 {ECO:0000313|EMBL:CAK13616.1, ECO:0000313|Proteomes:UP000000658};
RN [1] {ECO:0000313|EMBL:CAK13616.1, ECO:0000313|Proteomes:UP000000658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48 {ECO:0000313|EMBL:CAK13616.1,
RC ECO:0000313|Proteomes:UP000000658};
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(2006).
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|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; CT573326; CAK13616.1; -; Genomic_DNA.
DR RefSeq; WP_011532048.1; NC_008027.1.
DR AlphaFoldDB; Q1IFD8; -.
DR STRING; 384676.PSEEN0681; -.
DR GeneID; 32804002; -.
DR KEGG; pen:PSEEN0681; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_3_6; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000000658; Chromosome.
DR GO; GO:0016223; F:beta-alanine-pyruvate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
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; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42684:SF1; BETA-ALANINE--PYRUVATE AMINOTRANSFERASE; 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 Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:CAK13616.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Pyruvate {ECO:0000313|EMBL:CAK13616.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAK13616.1}.
SQ SEQUENCE 448 AA; 48401 MW; 639ED29D29E28712 CRC64;
MNMPENAQAG LASQLKLDAH WMPYTANRNF QRDPRLIVAA EGNYLVDDKG RKIFDALSGL
WTCGAGHTRK EISEAVARQV ATLDYSPAFQ FGHPLSFQLA EKIANLAPGD LNHVFFTNSG
SECADTALKM VRAYWRLKGQ ATKTKIIGRA RGYHGVNIAG TSLGGVNGNR KLFGQLLDVD
HLPHTVLPAN VFSKGMPEEG GIALADEMLK LIELHDASNI AAVIVEPLAG SAGVLPPPKG
YLKRLREICT QHNILLIFDE VITGFGRMGA MTGAEAFGVT PDLMCIAKQV TNGAIPMGAV
VATGEIYQTF MNQPTPEYAV EFPHGYTYSA HPVACAAGIA ALDLLQKENL VQSAAELAPH
FEKLLHGVKG TKNVVDIRNY GLAGAIQIAA RDGDAIVRPY EAAMKLWQAG FYVRFGGDTL
QFGPTFNTQP QELDRLFDAV GEALNKVD
//
