ID   A0A0Q5HD94_9BURK        Unreviewed;       482 AA.
AC   A0A0Q5HD94;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:KQQ87265.1};
GN   ORFNames=ASF77_16910 {ECO:0000313|EMBL:KQQ87265.1};
OS   Massilia sp. Leaf139.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1736272 {ECO:0000313|EMBL:KQQ87265.1, ECO:0000313|Proteomes:UP000051760};
RN   [1] {ECO:0000313|EMBL:KQQ87265.1, ECO:0000313|Proteomes:UP000051760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ87265.1,
RC   ECO:0000313|Proteomes:UP000051760};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ87265.1, ECO:0000313|Proteomes:UP000051760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ87265.1,
RC   ECO:0000313|Proteomes:UP000051760};
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   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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:KQQ87265.1}.
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DR   EMBL; LMOJ01000025; KQQ87265.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q5HD94; -.
DR   STRING; 1736272.ASF77_16910; -.
DR   OrthoDB; 3398487at2; -.
DR   Proteomes; UP000051760; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42684:SF3; GAMMA-AMINOBUTYRATE TRANSAMINASE POP2, MITOCHONDRIAL; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:KQQ87265.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051760};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KQQ87265.1}.
SQ   SEQUENCE   482 AA;  51904 MW;  455775213629D8C2 CRC64;
     MATDDTAVLA ASMVSAGIPD AETFDTRAIQ ARDAAHFLHP FTDHAALRTR GARVIVRGQG
     VYLWDSEGRQ LIDGMSGLWC VNVGYGRTSI SQAVYRQMET LPFYNSFFNT TNVPAVQLAT
     ELVALSPPQF SHVFFTGSGS EANDTIVRMV RRYWDILGQP ERQVIVSRKN AYHGSTMAGA
     SLGGMAGMHA QGGLPIPGIR HIGQPNYAEH GHGLSENAFG LVAAGWLEDE ILAVGPDKVA
     AFIGEPVQGA GGVIIPPPTY WPEVQRICDK YGILLVADEV ICGFGRLGAW FGSELMGMRP
     DLISFAKGVT SGYVPLGGVL VGKRVAQALV EQGGDFNHGF TYSGHPVACA AALENLRILR
     EERLVEKVAL ETGPYLKAAF NELATHPLVG HAESCGMVAG LNLVRRKGSG PHDCERFASD
     LQVGMVCRGH MFDNGVIMRA VGDRMIVAPP LVMSKTEIDE MAARIRDCLD LTLADIQARG
     WM
//