ID   A4Y6L2_SHEPC            Unreviewed;       404 AA.
AC   A4Y6L2;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=Sputcn32_1872 {ECO:0000313|EMBL:ABP75595.1};
OS   Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=319224 {ECO:0000313|EMBL:ABP75595.1};
RN   [1] {ECO:0000313|EMBL:ABP75595.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN-32 {ECO:0000313|EMBL:ABP75595.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella putrefaciens CN-32.";
RL   Submitted (APR-2007) 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; CP000681; ABP75595.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4Y6L2; -.
DR   STRING; 319224.Sputcn32_1872; -.
DR   KEGG; spc:Sputcn32_1872; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_6; -.
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:ABP75595.1};
KW   Transferase {ECO:0000313|EMBL:ABP75595.1}.
FT   DOMAIN          35..392
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   404 AA;  45444 MW;  03992E724439A76B CRC64;
     MRPIIKSNKL DSVCYDIRGP VHKEARRLED EGHRILKLNI GNPAPFGFEA PEEIVRDVIL
     NLPSAQGYCE SKGLFSARKA IVQYYQSLGI FGVDIEDIYI GNGVSELIMM AMQGLLNTDD
     EILIPSPDYP LWTAAANLAG GKAVHYRCDE EADWFPDLND IKSKISSRTR GIVLINPNNP
     TGAVYSRELL LQVVELCRQH DLILFADEIY DKILYDEAKH IPAAGLSDDI LTVTFNGLSK
     AYRAAGFRVG WMMLSGNLKA AKSYIEGLEM LSSMRLCANV PNQHAIQTAL GGYQSINELI
     LPNGRLTVQR DACYELLNQI PGVSVKKPKG ALYAFPKLDM KKFNLRDDER LVLDLLREKK
     ILLVHGSAFN WPEPDHLRVV FLPYKEDLNK ALTEFGDFLE NYRQ
//