ID   C6CEE3_DICC1            Unreviewed;       404 AA.
AC   C6CEE3;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=Dd1591_1391 {ECO:0000313|EMBL:ACT06253.1};
OS   Dickeya chrysanthemi (strain Ech1591) (Dickeya zeae (strain Ech1591)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=561229 {ECO:0000313|EMBL:ACT06253.1, ECO:0000313|Proteomes:UP000002735};
RN   [1] {ECO:0000313|EMBL:ACT06253.1, ECO:0000313|Proteomes:UP000002735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ech1591 {ECO:0000313|EMBL:ACT06253.1,
RC   ECO:0000313|Proteomes:UP000002735};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Dickeya zeae Ech1591.";
RL   Submitted (JUN-2009) 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; CP001655; ACT06253.1; -; Genomic_DNA.
DR   RefSeq; WP_012769130.1; NC_012912.1.
DR   AlphaFoldDB; C6CEE3; -.
DR   STRING; 561229.Dd1591_1391; -.
DR   KEGG; dze:Dd1591_1391; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_6; -.
DR   OrthoDB; 9803354at2; -.
DR   Proteomes; UP000002735; 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   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:ACT06253.1};
KW   Transferase {ECO:0000313|EMBL:ACT06253.1}.
FT   DOMAIN          34..390
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   404 AA;  45558 MW;  A66A9EFA8FACCB78 CRC64;
     MLPIEKSKKL ENVCYDIRGP VLKEAKRLEE EGNKVLKLNI GNPAPFGFEA PDEILVDVIR
     NLPTAQGYCD SKGLYSARKA IVQHYQARDM RDITLEDVYI GNGVSELIVQ SMQALLNTGD
     EMLVPAPDYP LWTAAVSLSN GHAVHYRCDE ESGWFPDLDD IRSKITPRTR GIVIINPNNP
     TGAVYSKELL LEVVEIARQH SLIIFADEIY DKILYDDAQH HSIAALAPDL LTVTFNGLSK
     TYRVAGFRQG WMVLNGPKKH ARGYIEGLEM LASMRLCANV PMQHAIQTAL GGYQSISEFI
     HPGGRLYEQR NRAWELINQI PGVSCVKPSG ALYMFPRIDA KRFNIHDDQK LVLDLLLQEK
     VLLVQGTAFN WPEPDHLRIV TLPRVDELEM AINKFGRFLE GYHQ
//