ID   B0KUP9_PSEPG            Unreviewed;       403 AA.
AC   B0KUP9;
DT   18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT   18-MAR-2008, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=PputGB1_1447 {ECO:0000313|EMBL:ABY97354.1};
OS   Pseudomonas putida (strain GB-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869 {ECO:0000313|EMBL:ABY97354.1, ECO:0000313|Proteomes:UP000002157};
RN   [1] {ECO:0000313|EMBL:ABY97354.1, ECO:0000313|Proteomes:UP000002157}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-1 {ECO:0000313|EMBL:ABY97354.1,
RC   ECO:0000313|Proteomes:UP000002157};
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., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT   "Complete sequence of Pseudomonas putida GB-1.";
RL   Submitted (JAN-2008) 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-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR   EMBL; CP000926; ABY97354.1; -; Genomic_DNA.
DR   RefSeq; WP_012271123.1; NC_010322.1.
DR   AlphaFoldDB; B0KUP9; -.
DR   KEGG; ppg:PputGB1_1447; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_6; -.
DR   Proteomes; UP000002157; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43488; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR   PANTHER; PTHR43488:SF2; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ABY97354.1};
KW   Transferase {ECO:0000313|EMBL:ABY97354.1}.
FT   DOMAIN          34..390
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   403 AA;  44711 MW;  4A40AAC073E2BD98 CRC64;
     MQFSKSNKLA NVCYDIRGPV LKHAKRLEEE GHRILKLNIG NPAPFGFEAP DEILQDVIRN
     LPTAQGYSDS KGLFSARKAV MQYCQQKEIE GVTIEDIYLG NGVSELIVMS MQALLNNGDE
     VLIPAPDYPL WTAAVSLAGG KPVHYLCDEQ ADWFPDLEDI KAKITPNTKA LVIINPNNPT
     GAVYSKELLL GMLELARQHN LVVFSDEIYD KILYDEAVHI STASLAPDLL CLTFNGLSKS
     YRVAGFRSGW LIISGPKHHA QSYIEGIDML ANMRLCANVP AQHAIQTALG GYQSINDLVL
     PPGRLLEQRN RTYELLNDIP GVSCVKPMGA LYAFPRIDPK VCPILNDEKF ALDLLLSEKL
     LIVQGTAFNW PWPDHFRVVT LPRVDDLEAA IGRIGNFLKG YSQ
//