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Database: UniProt
Entry: A0A0S9NQE0_9BURK
LinkDB: A0A0S9NQE0_9BURK
Original site: A0A0S9NQE0_9BURK 
ID   A0A0S9NQE0_9BURK        Unreviewed;       387 AA.
AC   A0A0S9NQE0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=ASF44_22795 {ECO:0000313|EMBL:KQP47516.1};
OS   Pseudorhodoferax sp. Leaf274.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae.
OX   NCBI_TaxID=1736318 {ECO:0000313|EMBL:KQP47516.1, ECO:0000313|Proteomes:UP000051759};
RN   [1] {ECO:0000313|EMBL:KQP47516.1, ECO:0000313|Proteomes:UP000051759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf274 {ECO:0000313|EMBL:KQP47516.1,
RC   ECO:0000313|Proteomes:UP000051759};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQP47516.1, ECO:0000313|Proteomes:UP000051759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf274 {ECO:0000313|EMBL:KQP47516.1,
RC   ECO:0000313|Proteomes:UP000051759};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KQP47516.1}.
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DR   EMBL; LMNA01000003; KQP47516.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S9NQE0; -.
DR   STRING; 1736318.ASF44_22795; -.
DR   OrthoDB; 9803354at2; -.
DR   Proteomes; UP000051759; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; 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   PANTHER; PTHR46383:SF2; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 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   ECO:0000313|EMBL:KQP47516.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051759};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KQP47516.1}.
FT   DOMAIN          35..377
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   387 AA;  42429 MW;  2F672F6097B1202D CRC64;
     MRKAIQDLAE SQIREVANAG IGRDDVLPFW FGESDEVTPE FIRQAAIESL QRGETFYAHN
     LGLPELREAI ARYMSALHGP IPAERIAVTS GGVNALMLAV QCLVDPGDEV VAVTPVWPNL
     TAQPAIMGAR LRCVPLRPVD GQWTLDLEAL LAAITPATRM LIVNAPNNPT GWTLRAEEQA
     ALLAHCRRTG TWILADEVYE RLYYADAPGA CAPSFLDQAQ PDDRLVVVHS FSKSFLMTGW
     RLGWLVMPAT LVQAMGKLIE FNTSCASVFT QRAALAALAR QDEVTPRVVA HLRLCRDTLV
     PLLAAMPQVA VSAAHGGMYA FFRLECADDS LAVAKRLVRE AGLGLAPGTA FAPEAQGWLR
     WCFASRDPQR LVLGAERLDR WLRQRNA
//
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