ID   D2BS43_DICZ5            Unreviewed;       404 AA.
AC   D2BS43;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=Dd586_2750 {ECO:0000313|EMBL:ACZ77590.1};
OS   Dickeya zeae (strain Ech586) (Dickeya dadantii (strain Ech586)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya; Dickeya parazeae.
OX   NCBI_TaxID=590409 {ECO:0000313|EMBL:ACZ77590.1, ECO:0000313|Proteomes:UP000001446};
RN   [1] {ECO:0000313|EMBL:ACZ77590.1, ECO:0000313|Proteomes:UP000001446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ech586 {ECO:0000313|EMBL:ACZ77590.1,
RC   ECO:0000313|Proteomes:UP000001446};
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., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Dickeya dadantii Ech586.";
RL   Submitted (DEC-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; CP001836; ACZ77590.1; -; Genomic_DNA.
DR   RefSeq; WP_012885401.1; NC_013592.1.
DR   AlphaFoldDB; D2BS43; -.
DR   STRING; 590409.Dd586_2750; -.
DR   GeneID; 60869018; -.
DR   KEGG; ddc:Dd586_2750; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_6; -.
DR   OrthoDB; 9803354at2; -.
DR   Proteomes; UP000001446; 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:ACZ77590.1};
KW   Transferase {ECO:0000313|EMBL:ACZ77590.1}.
FT   DOMAIN          34..390
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   404 AA;  45504 MW;  6804623801252528 CRC64;
     MSPIEKSKKL ENVCYDIRGP VLKEAKRLEE EGNKVLKLNI GNPAPFGFDA PDEILVDVIR
     NLPTAQGYCD SKGLYSARKA IVQHYQARDM RDVTLEDVYI GNGVSELIVQ SMQALLNTGD
     EMLVPAPDYP LWTAAVSLSS GNAVHYRCDE ESDWFPDLDD IRSKITPRTR GIVIINPNNP
     TGAVYSKELL LEVVEIARQH NLIIFADEIY DKILYDDAQH HSIAALAPDL LTVTFNGLSK
     TYRVAGFRQG WMVLNGPKKH ARGYIEGLEM LASMRLCANV PMQHAIQTAL GGYQSISEFI
     HPGGRLYEQR NRAWELINQI PGVSCVKPNG ALYMFPRIDA KRFNIHDDQK LVLDLLLQEK
     VLLVQGTAFN WPEPDHLRIV TLPRVDDLDM AINKLGRFLE GYHQ
//