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
//