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
//