ID   Q8L3K9_TETHA            Unreviewed;       532 AA.
AC   Q8L3K9;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   Name=aspD {ECO:0000313|EMBL:BAB92080.1};
OS   Tetragenococcus halophilus (Pediococcus halophilus).
OG   Plasmid pD1 {ECO:0000313|EMBL:BAB92080.1}.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Tetragenococcus.
OX   NCBI_TaxID=51669 {ECO:0000313|EMBL:BAB92080.1};
RN   [1] {ECO:0000313|EMBL:BAB92080.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=D10 {ECO:0000313|EMBL:BAB92080.1};
RC   PLASMID=pD1 {ECO:0000313|EMBL:BAB92080.1};
RX   PubMed=12003930; DOI=10.1128/JB.184.11.2906-2913.2002;
RA   Abe K., Ohnishi F., Yagi K., Nakajima T., Higuchi T., Sano M., Machida M.,
RA   Sarker R.I., Maloney P.C.;
RT   "Plasmid-encoded asp operon confers a proton motive metabolic cycle
RT   catalyzed by an aspartate-alanine exchange reaction.";
RL   J. Bacteriol. 184:2906-2913(2002).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU000481};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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DR   EMBL; AB072729; BAB92080.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8L3K9; -.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 1.10.20.110; -; 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; IPR022518; Aspartate_4-decarboxylase.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR03801; asp_4_decarbox; 1.
DR   PANTHER; PTHR43795:SF10; AMINOTRAN_1_2 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43795; BIFUNCTIONAL ASPARTATE AMINOTRANSFERASE AND GLUTAMATE/ASPARTATE-PREPHENATE AMINOTRANSFERASE-RELATED; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU000481};
KW   Plasmid {ECO:0000313|EMBL:BAB92080.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Transferase {ECO:0000256|RuleBase:RU000481}.
FT   DOMAIN          160..333
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   532 AA;  60073 MW;  119F39E41DBC4BD6 CRC64;
     MESLDIEQLK GMSNFEVAAL FLENSEKNTM HNTPINVGRG NPNWINTRAR LAFNKIAEFG
     IGESAKTIDE ADGDMAGYVE KEGIAQRLHD YLDANDKTDK FILDFLAYTE NNMHLNQDDL
     VHEFVDGAIG NHYPVPSRSL VNVEKILNKY LEVSLYNGEK LADHTNVFPT EGGTAAMVYL
     FNELKISHIL EAGDTIAINT PIFTPYLQIP ELSEFKLKEL DVSSVEDNNW QMLDAKFEEL
     KDPSVKAFFV VNPTNPTSRA FSQHALDKIK EVVAANPEII IITDDVYGTF VNNFQTIYSV
     APKNTLLVYS YSKLYGATGH RLGLIAAHED NVFDEIIAKR TAENAAIKEE FEKRYSLVVA
     NPLDMKFIDR TVADSREIGL YHTAGLSTPQ QVLMALFSLT NLIHEGEKDP YIEASKKVVD
     VRYNTFWKSM GIEGDHSAEK AEYYTVFNIY ELAEKKYGKN FRDYFENNFS YLEFEGELAG
     KYGVVAMDGA GMGTEEGYLR VSLANQPAEN YTITGKRIAE LLAEYYDKFQ QK
//