ID J2L4I9_9SPHN Unreviewed; 403 AA.
AC J2L4I9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Aspartate/tyrosine/aromatic aminotransferase {ECO:0000313|EMBL:EJK82291.1};
GN ORFNames=PMI04_02677 {ECO:0000313|EMBL:EJK82291.1};
OS Sphingobium sp. AP49.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1144307 {ECO:0000313|EMBL:EJK82291.1};
RN [1] {ECO:0000313|EMBL:EJK82291.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP49 {ECO:0000313|EMBL:EJK82291.1};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:EJK82291.1}.
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DR EMBL; AJVL01000059; EJK82291.1; -; Genomic_DNA.
DR AlphaFoldDB; J2L4I9; -.
DR STRING; 1144307.PMI04_02677; -.
DR PATRIC; fig|1144307.3.peg.2442; -.
DR eggNOG; COG1448; Bacteria.
DR OrthoDB; 9766445at2; -.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:amino acid metabolic process; 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; IPR000796; Asp_trans.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11879; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR11879:SF22; ASPARTATE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EJK82291.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transferase {ECO:0000313|EMBL:EJK82291.1}.
FT DOMAIN 41..393
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 403 AA; 41834 MW; 6E7007CB11D20732 CRC64;
MTDTTLLAPA PGRSLFGALD RQAPDALLGL IAQYRADPRA DKMDLGVGVY RDEAGATPVM
RAVKAAEAVL LAEQGSKSYL GPEGDTGFVD LLAAIVFGPL AGSDRIAGVQ TPGGTGALRL
GADLIARARP GATVWIGDPT WPNHAPIFRE AGLTLAPHRF LDGAGAVDFD AMLADLAAAQ
AGDVLLLHGC CHNPTGVDFS AEQWAAIADL CAARGLIPFI DLAYQGLGDG LEADAAATRQ
MLAAVPDALV AYSCDKNFGL YRERVGALWV QGANAALTTL AFSNIVALAR GIWSMPPDHG
AAIVRTILER PAMRAEWTGE LDQMRTRINA LRAALAAAHP QLAAIAGQRG MFAMLPVSAA
AVAAMRADHG IYMAGNGRIN IAGLRLDTIP AFVAGLSPHL PSA
//
