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Database: UniProt
Entry: A0A162SUD1_9CLOT
LinkDB: A0A162SUD1_9CLOT
Original site: A0A162SUD1_9CLOT 
ID   A0A162SUD1_9CLOT        Unreviewed;       394 AA.
AC   A0A162SUD1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=2-aminoadipate transaminase {ECO:0000313|EMBL:KZL91880.1};
DE            EC=2.6.1.39 {ECO:0000313|EMBL:KZL91880.1};
GN   Name=lysN_3 {ECO:0000313|EMBL:KZL91880.1};
GN   ORFNames=CLMAG_16860 {ECO:0000313|EMBL:KZL91880.1};
OS   Clostridium magnum DSM 2767.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121326 {ECO:0000313|EMBL:KZL91880.1, ECO:0000313|Proteomes:UP000076603};
RN   [1] {ECO:0000313|EMBL:KZL91880.1, ECO:0000313|Proteomes:UP000076603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2767 {ECO:0000313|EMBL:KZL91880.1,
RC   ECO:0000313|Proteomes:UP000076603};
RA   Poehlein A., Uhlig R., Fischer R., Bahl H., Daniel R.;
RT   "Genome sequence of Clostridium magnum DSM 2767.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZL91880.1}.
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DR   EMBL; LWAE01000002; KZL91880.1; -; Genomic_DNA.
DR   RefSeq; WP_066620788.1; NZ_LWAE01000002.1.
DR   AlphaFoldDB; A0A162SUD1; -.
DR   STRING; 1121326.CLMAG_16860; -.
DR   PATRIC; fig|1121326.3.peg.1666; -.
DR   OrthoDB; 9802328at2; -.
DR   Proteomes; UP000076603; Unassembled WGS sequence.
DR   GO; GO:0047536; F:2-aminoadipate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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; PTHR42790; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42790:SF19; AROMATIC AMINO ACID AMINOTRANSFERASE DDB_G0272014; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000313|EMBL:KZL91880.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076603};
KW   Transferase {ECO:0000313|EMBL:KZL91880.1}.
FT   DOMAIN          41..385
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   394 AA;  45101 MW;  1B4BBF4CF8F22EEF CRC64;
     MNNKFAKRTQ NLKPSEVREI LKVTERPEVI SFAGGLPAPE LFPIEEIKKA CIEVLNDKGQ
     SALQYSTTEG YVPLREAICG RMKNLGIEAS IDNVIVTTGS QQALDLSGKL FIDEGDTIIC
     ESPTYLAAIN AFKAYMPKFQ EVAMDEEGMI MEELEKTLID NPNAKFIYTI PDFQNPTGRT
     MSLSRRKKLV ELANQYNIVI IEDNPYGEVR FAGEKLPPVK HFDTEGRVIY LSTFSKIFAP
     GLRLGWICAD KEFIDKYVPF KQNIDLHSDI FAQMITAKYM ELFDIEAHIE KIREVYRHRR
     ELMIKCIKEE FPENIKYTLP DGGLFIWVQL PDNVDASELF VKALENNVVF VSGQSFFPNG
     NYKNAFRLNY SNMPDERIVE GIKRLAEVIK EYKN
//
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