ID   A0A1X1EL62_PANCY        Unreviewed;       284 AA.
AC   A0A1X1EL62;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=D-amino acid aminotransferase {ECO:0000313|EMBL:ORM89667.1};
GN   ORFNames=HA50_23975 {ECO:0000313|EMBL:ORM89667.1};
OS   Pantoea cypripedii (Pectobacterium cypripedii) (Erwinia cypripedii).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=55209 {ECO:0000313|EMBL:ORM89667.1, ECO:0000313|Proteomes:UP000193749};
RN   [1] {ECO:0000313|EMBL:ORM89667.1, ECO:0000313|Proteomes:UP000193749}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 2657 {ECO:0000313|EMBL:ORM89667.1,
RC   ECO:0000313|Proteomes:UP000193749};
RX   PubMed=28255640;
RA   Palmer M., Steenkamp E.T., Coetzee M.P., Chan W.Y., van Zyl E.,
RA   De Maayer P., Coutinho T.A., Blom J., Smits T.H., Duffy B., Venter S.N.;
RT   "Phylogenomic resolution of the bacterial genus Pantoea and its
RT   relationship with Erwinia and Tatumella.";
RL   Antonie Van Leeuwenhoek 0:0-0(2017).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU004516};
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009320,
CC       ECO:0000256|RuleBase:RU004106}.
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:ORM89667.1}.
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DR   EMBL; MLJI01000002; ORM89667.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1EL62; -.
DR   STRING; 55209.HA50_23975; -.
DR   OrthoDB; 21319at2; -.
DR   Proteomes; UP000193749; Unassembled WGS sequence.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046394; P:carboxylic acid biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd01558; D-AAT_like; 1.
DR   Gene3D; 3.30.470.10; -; 1.
DR   Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 1.
DR   InterPro; IPR001544; Aminotrans_IV.
DR   InterPro; IPR018300; Aminotrans_IV_CS.
DR   InterPro; IPR036038; Aminotransferase-like.
DR   InterPro; IPR043132; BCAT-like_C.
DR   InterPro; IPR043131; BCAT-like_N.
DR   PANTHER; PTHR42743; AMINO-ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42743:SF10; D-ALANINE AMINOTRANSFERASE; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ORM89667.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004516}; Transferase {ECO:0000313|EMBL:ORM89667.1}.
SQ   SEQUENCE   284 AA;  31375 MW;  45BBA58FECBD0176 CRC64;
     MRTVYLNGEF IAENEAKISV FDRGFTFADA IYEVTAVLQG RLVDFEQHLK RLRRSLGELA
     LSLPVDNDQL LAIHRELITR NDLHEGLIYL QVSRGVEDRN FSFPAAGTPP TLVLYTQAKD
     ILGSPLAKRG MNIISLPDLR WGRCDIKTTQ LLYACLAKEQ ARLRGADDAW LVKDGLITEG
     TSNNAFIITH AGAVVTRELS QLLLPGITRS ALIALINEHG LRLEERGFTI DEVREAAEAF
     ITSSTSFVYP VVNVDGQPVG AGQPGPLTQR LRQLYIEHAL AAAL
//