ID A0A0M2R7R2_9PROT Unreviewed; 400 AA.
AC A0A0M2R7R2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=aspartate transaminase {ECO:0000256|ARBA:ARBA00012753};
DE EC=2.6.1.1 {ECO:0000256|ARBA:ARBA00012753};
GN ORFNames=WH95_04330 {ECO:0000313|EMBL:KKJ77686.1};
OS Kiloniella litopenaei.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Kiloniellaceae; Kiloniella.
OX NCBI_TaxID=1549748 {ECO:0000313|EMBL:KKJ77686.1, ECO:0000313|Proteomes:UP000034491};
RN [1] {ECO:0000313|EMBL:KKJ77686.1, ECO:0000313|Proteomes:UP000034491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1-1 {ECO:0000313|EMBL:KKJ77686.1,
RC ECO:0000313|Proteomes:UP000034491};
RA Shao Z., Wang L., Li X.;
RT "Genome sequence of Kiloniella sp. P1-1, isolated from the gut microflora
RT of Pacific white shrimp, Penaeus vannamei.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000984};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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:KKJ77686.1}.
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DR EMBL; LANI01000003; KKJ77686.1; -; Genomic_DNA.
DR RefSeq; WP_046503527.1; NZ_LANI01000003.1.
DR AlphaFoldDB; A0A0M2R7R2; -.
DR STRING; 1549748.WH95_04330; -.
DR PATRIC; fig|1549748.8.peg.2345; -.
DR OrthoDB; 9763453at2; -.
DR Proteomes; UP000034491; Unassembled WGS sequence.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase 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; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KKJ77686.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034491};
KW Transferase {ECO:0000313|EMBL:KKJ77686.1}.
FT DOMAIN 32..392
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 400 AA; 43427 MW; 3342C0FE0D2626A0 CRC64;
MPQLADRLSR IKPSPTIAVT TKARELKAAG RDVIGLGAGE PDFDTPDNIK AAAITAINGG
DTRYTAVDGT PELKAAICEK FKRDNGLDYK PEQITVGTGG KQILYNAFMA TLNPGDEVII
PAPFWVSYPD MVLLADGEPV AVPCMQSNGF KLQAEDLEEA ITDKTKWVLL NSPSNPTGAA
YSYDEMKALT DVLKRHEHVM ILTDDMYEKL VYDDFEFVTP AQVEPSLYDR TLTMNGVSKA
YCMTGWRIGF AGGPTALIKA MAKIQSQSTS NPCSVSQAAA VEALRGDQSF IPKHNEVFKA
RRDMVVDLLN DCPGINCSKP EGAFYVYPSC EGTIGKTTPD GKQISSDGDF VTYLLEGFDV
AAVQGEAFGL SPYFRISYAT STEALKEACE RIKRACEALS
//
