ID   A4XP50_PSEMY            Unreviewed;       457 AA.
AC   A4XP50;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:ABP83116.1};
DE            EC=2.6.1.- {ECO:0000313|EMBL:ABP83116.1};
GN   OrderedLocusNames=Pmen_0343 {ECO:0000313|EMBL:ABP83116.1};
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739 {ECO:0000313|EMBL:ABP83116.1};
RN   [1] {ECO:0000313|EMBL:ABP83116.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ymp {ECO:0000313|EMBL:ABP83116.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Hersman L., Dubois J., Maurice P., Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-2007) 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}.
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DR   EMBL; CP000680; ABP83116.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4XP50; -.
DR   STRING; 399739.Pmen_0343; -.
DR   KEGG; pmy:Pmen_0343; -.
DR   PATRIC; fig|399739.8.peg.352; -.
DR   eggNOG; COG0161; Bacteria.
DR   HOGENOM; CLU_016922_4_1_6; -.
DR   OrthoDB; 9801052at2; -.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0071704; P:organic substance 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; PTHR43094; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 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:0000313|EMBL:ABP83116.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:ABP83116.1}.
SQ   SEQUENCE   457 AA;  50154 MW;  CDDFD7BE6733E19D CRC64;
     MNKQANNPQT AHWQALSQAH HLAPFSDYKQ LAEKGPRIIT EAKGVHLWDS EGNKILDGMA
     GLWCVAVGYG REELVEAAAT QMRQLPFYNT FFQTAHPPVL ELAHAISQLA PAGMNHVFFT
     GSGSEGNDTM LRLVRHYWAC KGKASKKIII GRENGYHGST VAGASLGGMK FMHEQGDLPI
     PGIAHIPQPY WFGEGGDQSP EEFGIWAADQ LEKKILELGE ENVAAFIAEP IQGAGGVIIP
     PETYWPRIKE ILAKYDILFV ADEVICGFGR TGEWFGSQYY DLKPDLMTIA KGLTSGYVPM
     GGLIVSDKVF EVIEAHGDFN HGFTYSGHPV AAAVGLENLR LLREEGIVER VKAETAPYLQ
     QRLRELADHP LVGEVRGLGM LGAIELVQDK ATRKRYPDTV AAGMVCRGHC FNNGLIMRAV
     GDTMIIAPPL VISRAEIDEL VEKARKCLDL TLRDLSV
//