ID A0A0X1T5C8_PSEAA Unreviewed; 449 AA.
AC A0A0X1T5C8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Omega amino acid--pyruvate aminotransferase {ECO:0000313|EMBL:AMB87277.1};
GN ORFNames=AWM79_19060 {ECO:0000313|EMBL:AMB87277.1};
OS Pseudomonas agarici.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=46677 {ECO:0000313|EMBL:AMB87277.1, ECO:0000313|Proteomes:UP000063229};
RN [1] {ECO:0000313|EMBL:AMB87277.1, ECO:0000313|Proteomes:UP000063229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 2472 {ECO:0000313|EMBL:AMB87277.1,
RC ECO:0000313|Proteomes:UP000063229};
RA McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA SanMiguel P., Csonka L.;
RL Submitted (JAN-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 -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CP014135; AMB87277.1; -; Genomic_DNA.
DR RefSeq; WP_060783539.1; NZ_CP014135.1.
DR AlphaFoldDB; A0A0X1T5C8; -.
DR STRING; 46677.AWM79_19060; -.
DR Proteomes; UP000063229; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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:AMB87277.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Pyruvate {ECO:0000313|EMBL:AMB87277.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000063229};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AMB87277.1}.
SQ SEQUENCE 449 AA; 48628 MW; A60ABE08D2F38CA4 CRC64;
MNMPENAPSS LASQLKLDAH WMPYTANRNF QRDPRLIVAA EGSWLIDDKG RKIYDSLSGL
WTCGAGHTRK EIQEAVARQL GTLDYSPGFQ YGHPLSFQLA EKITALTPGN LNHVFFTNSG
SECADTAVKM VRAYWRLKGQ ATKTKMIGRA RGYHGVNIAG TSLGGVNGNR KLFGQAMMDV
DHLPHTLLAS NAFSRGMPEQ GGIALADELL KLIELHDASN IAAVFVEPLA GSAGVLVPPQ
GYLKRLREIC DQHNILLVFD EVITGFGRTG AMFGATSFGV TPDLMCIAKQ ITNGAIPMGA
VIASSEIYQT FMNQPTPEYA VEFPHGYTYS AHPVACAAGL ASLELLQKEN LVQSVAELAP
HFESALHGLK GGKNVIDIRN YGLAGAIQIA SRDGDAIVRP FEAGMALWKA GFYVRFGGDT
LQFGPTFNSR PQDLDRLFDA VGEVLNKLD
//