ID A0A0S8E7U0_9BACT Unreviewed; 387 AA.
AC A0A0S8E7U0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Aspartate aminotransferase {ECO:0000313|EMBL:KPK43372.1};
DE EC=2.6.1.1 {ECO:0000313|EMBL:KPK43372.1};
GN ORFNames=AMJ65_05970 {ECO:0000313|EMBL:KPK43372.1};
OS Phycisphaerae bacterium SG8_4.
OC Bacteria; Planctomycetota; Phycisphaerae.
OX NCBI_TaxID=1703409 {ECO:0000313|EMBL:KPK43372.1, ECO:0000313|Proteomes:UP000051853};
RN [1] {ECO:0000313|EMBL:KPK43372.1, ECO:0000313|Proteomes:UP000051853}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_4 {ECO:0000313|EMBL:KPK43372.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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:KPK43372.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJTR01000081; KPK43372.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8E7U0; -.
DR PATRIC; fig|1703409.3.peg.3598; -.
DR Proteomes; UP000051853; 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:SF6; AMINOTRAN_1_2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Aminotransferase {ECO:0000313|EMBL:KPK43372.1};
KW Transferase {ECO:0000313|EMBL:KPK43372.1}.
FT DOMAIN 29..373
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 387 AA; 42711 MW; 09598E17721A5D16 CRC64;
MYDSLRMQSV QSPIIPVVGE LIRNNPGTIS LGQGVAYYWP PPEAIAGIQK FIADPANHKY
KLVQGIPELQ AAIAHKLSTE NNISLDGSRI VVTAGANMGF VNAVLAIADP GDEIILQLPY
YFNHEMAVTI ADCKAVCVPA DDDYQLQPDS IASAITDRTR AVVTISPNNP TGAVYRESDL
REVNAHCRRN GIYHISDEAY EYFTYDGAKH FSPGSIDDSA GHTISLFSLS KAYGFASWRI
GWMVRPERLY MSVRKIQDTI LICPPVISQW AAVGAMEAGR RYCLEKQQMT ADIRRMVLER
LNDIADLVTV PRADGAFYLL LRVHKDTNPM ELVSQLIEEH KVAVIPGMTF GMEDKCYLRV
AYGALHKETA AEGIGRLVEG LGHILAT
//