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Database: UniProt/TrEMBL
Entry: A0A0R2HLC9_9LACO
LinkDB: A0A0R2HLC9_9LACO
Original site: A0A0R2HLC9_9LACO 
ID   A0A0R2HLC9_9LACO        Unreviewed;       430 AA.
AC   A0A0R2HLC9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Pyridoxal phosphate-dependent aminotransferase {ECO:0000313|EMBL:AMV67121.1};
GN   ORFNames=ADU72_1188 {ECO:0000313|EMBL:AMV67121.1};
OS   Pediococcus damnosus.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=51663 {ECO:0000313|EMBL:AMV67121.1, ECO:0000313|Proteomes:UP000076244};
RN   [1] {ECO:0000313|EMBL:AMV67121.1, ECO:0000313|Proteomes:UP000076244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMW 2.1535 {ECO:0000313|EMBL:AMV67121.1,
RC   ECO:0000313|Proteomes:UP000076244};
RX   PubMed=27028007;
RA   Behr J., Geissler A.J., Schmid J., Zehe A., Vogel R.F.;
RT   "The Identification of Novel Diagnostic Marker Genes for the Detection of
RT   Beer Spoiling Pediococcus damnosus Strains Using the BlAst Diagnostic Gene
RT   findEr.";
RL   PLoS ONE 11:E0152747-E0152747(2016).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP012288; AMV67121.1; -; Genomic_DNA.
DR   RefSeq; WP_052694468.1; NZ_NAER01000002.1.
DR   STRING; 51663.ADU72_1188; -.
DR   GeneID; 57276308; -.
DR   KEGG; pdm:ADU72_1188; -.
DR   PATRIC; fig|51663.50.peg.1633; -.
DR   OrthoDB; 9807885at2; -.
DR   Proteomes; UP000076244; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:AMV67121.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:AMV67121.1}.
SQ   SEQUENCE   430 AA;  46968 MW;  1D377C1C47747DA4 CRC64;
     MSQSKNPERQ RLIAIDHQYV APAGRVSKFD LVVDHGKGAK VWDVDGNVYI DFLASASAVN
     VGHSNPKVVA AIHNQTDKLI HYISGYFYHE PAIKLAKRLA LLAPGKTPKK VSFSTSGSEA
     AEAVVKFARS YTKRSVILTF QNSWHGTTLG AASLSAIDGN MHRDIGPLIP DIHHIPFPNP
     DKRFPGESLA DFSKRYLKEL TDLFTRDIPA DQIAAILIEP IQGDAGIIMP PISYMQGLYK
     ICHENGILFC TDEINQGFGR SGKMWSIDHF NLEPDLMAVG KSLASGMPLS AIIGKAPIMD
     SLASPANATT TAANPICCAA ALATIDEIES LDLVERSRKL GEFSKTQFSK LQKEFPVIKH
     VRMIGLNGGI EFAEDQSQLV TNLCNYCFEH GLIVISTMDH IIRFQPPLVI TKAELTKGIG
     ILHDGLTNLV
//
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