ID   D3H1F5_ECO44            Unreviewed;       405 AA.
AC   D3H1F5;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-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=EC042_2531 {ECO:0000313|EMBL:CBG35363.1};
OS   Escherichia coli O44:H18 (strain 042 / EAEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=216592 {ECO:0000313|EMBL:CBG35363.1, ECO:0000313|Proteomes:UP000001407};
RN   [1] {ECO:0000313|EMBL:CBG35363.1, ECO:0000313|Proteomes:UP000001407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=042 / EAEC {ECO:0000313|Proteomes:UP000001407};
RX   PubMed=20098708; DOI=10.1371/journal.pone.0008801;
RA   Chaudhuri R.R., Sebaihia M., Hobman J.L., Webber M.A., Leyton D.L.,
RA   Goldberg M.D., Cunningham A.F., Scott-Tucker A., Ferguson P.R.,
RA   Thomas C.M., Frankel G., Tang C.M., Dudley E.G., Roberts I.S., Rasko D.A.,
RA   Pallen M.J., Parkhill J., Nataro J.P., Thomson N.R., Henderson I.R.;
RT   "Complete genome sequence and comparative metabolic profiling of the
RT   prototypical enteroaggregative Escherichia coli strain 042.";
RL   PLoS ONE 5:E8801-E8801(2010).
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; FN554766; CBG35363.1; -; Genomic_DNA.
DR   RefSeq; WP_000074530.1; NC_017626.1.
DR   AlphaFoldDB; D3H1F5; -.
DR   KEGG; elo:EC042_2531; -.
DR   PATRIC; fig|216592.3.peg.2647; -.
DR   HOGENOM; CLU_017584_4_2_6; -.
DR   Proteomes; UP000001407; 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:CBG35363.1};
KW   Transferase {ECO:0000313|EMBL:CBG35363.1}.
FT   DOMAIN          34..386
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   405 AA;  45545 MW;  7D7948904BF3C388 CRC64;
     MSPIEKSSKL ENVCYDIRGP VLKEAKRLEE EGNKVLKLNI GNPAPFGFDA PDEILVDVIR
     NLPTAQGYCD SKGLYSARKA IMQHYQARGM RDVTVEDIYI GNGVSELIVQ AMQALLNSGD
     EMLVPAPDYP LWTAAVSLSS GKAVHYLCDE SSDWFPDLDD IRAKITPRTR GIVIINPNNP
     TGAVYSKELL MEIVEIARQH NLIIFADEIY DKILYDDAEH HSIAPLAPDL LTITFNGLSK
     TYRVAGFRQG WMVLNGPKKH AKGYIEGLEM LASMRLCANV PAQHAIQTAL GGYQSISEFI
     TPGGRLYEQR NRAWELINDI PGVSCVKPRG ALYMFPKIDA RRFNIHDDQK MVLDFLLQEK
     VLLVQGTAFN WPWPDHFRIV TLPRVDDIEL SLSKFARFLS GYHQL
//