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Database: UniProt/TrEMBL
Entry: A0A0E3ZKL9_9BURK
LinkDB: A0A0E3ZKL9_9BURK
Original site: A0A0E3ZKL9_9BURK 
ID   A0A0E3ZKL9_9BURK        Unreviewed;       422 AA.
AC   A0A0E3ZKL9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=CL55_00014880 {ECO:0000313|EMBL:AKD25821.1};
OS   Polynucleobacter duraquae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=1835254 {ECO:0000313|EMBL:AKD25821.1, ECO:0000313|Proteomes:UP000061135};
RN   [1] {ECO:0000313|EMBL:AKD25821.1, ECO:0000313|Proteomes:UP000061135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWH-MoK4 {ECO:0000313|EMBL:AKD25821.1,
RC   ECO:0000313|Proteomes:UP000061135};
RA   Hahn M.W.;
RT   "Genome of Polynucleobacter strain MWH-MoK4.";
RL   Submitted (MAR-2014) 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; CP007501; AKD25821.1; -; Genomic_DNA.
DR   RefSeq; WP_046330530.1; NZ_CP007501.1.
DR   AlphaFoldDB; A0A0E3ZKL9; -.
DR   STRING; 1835254.CL55_00014880; -.
DR   KEGG; pdq:CL55_00014880; -.
DR   PATRIC; fig|576611.7.peg.1514; -.
DR   HOGENOM; CLU_017584_4_2_4; -.
DR   OrthoDB; 9803354at2; -.
DR   Proteomes; UP000061135; Chromosome.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009042; F:valine-pyruvate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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:AKD25821.1};
KW   Transferase {ECO:0000313|EMBL:AKD25821.1}.
FT   DOMAIN          34..394
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   422 AA;  46976 MW;  3729EAC246961A2B CRC64;
     MKPILKSAKL NHVCYDIRGP VLELAQRMEE EGHKIIKLNI GNVGVFGFDP PEEIQLDMIR
     NLGNASAYSD SKGIFAARKA IMQYCQEKGI QGVTLDDIYT GNGVSELIVL AMNALLNNGD
     EVLVPAPDYP LWTAAVSLSG GTPVHYLCDE SKEWAPDLAD LRKKITARTK AIVVINPNNP
     TGAIYSKEVL TELCSIAREH DLILFADEIY DKMLYDKEKH VSLASLSTDV VTITFNGLSK
     NYRSCGYRAG WMVVSGDKEM IRDYIEGLNM LSSMRLCANV PGQYAIQTAL GGYQSINDLV
     AEGGRLAKQR DLAWKLITEI PGVTCVKPKS ALYLFPKLDA EMYPIEDDQQ FVADFLKEEK
     VLLVQGSGFN WIKSDHFRVV FLPHEDVLKE AIGRLARFLE RYRQKHSRKA TSSTNSTATK
     AS
//
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