ID   A0A0Q9SIT7_9MICO        Unreviewed;       373 AA.
AC   A0A0Q9SIT7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Class V aminotransferase {ECO:0000313|EMBL:KRF27309.1};
GN   ORFNames=ASG91_12645 {ECO:0000313|EMBL:KRF27309.1};
OS   Phycicoccus sp. Soil802.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Phycicoccus.
OX   NCBI_TaxID=1736414 {ECO:0000313|EMBL:KRF27309.1, ECO:0000313|Proteomes:UP000050906};
RN   [1] {ECO:0000313|EMBL:KRF27309.1, ECO:0000313|Proteomes:UP000050906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil802 {ECO:0000313|EMBL:KRF27309.1,
RC   ECO:0000313|Proteomes:UP000050906};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRF27309.1, ECO:0000313|Proteomes:UP000050906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil802 {ECO:0000313|EMBL:KRF27309.1,
RC   ECO:0000313|Proteomes:UP000050906};
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   -!- 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:KRF27309.1}.
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; LMSS01000005; KRF27309.1; -; Genomic_DNA.
DR   RefSeq; WP_056922981.1; NZ_LMSS01000005.1.
DR   AlphaFoldDB; A0A0Q9SIT7; -.
DR   Proteomes; UP000050906; Unassembled WGS sequence.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000313|EMBL:KRF27309.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Transferase {ECO:0000313|EMBL:KRF27309.1}.
FT   DOMAIN          22..218
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   373 AA;  39933 MW;  E31E59BC5DFFBF9B CRC64;
     MTLPRADVDP DGLLEYSVVF TDRSLNHMSK RFVGAMQDII DVLRTTYSAH TVAVVPGGGT
     YAMEAVARQL ATGRRCLVVR NGLFSYRWSQ ILDAGSVAED VTVCRARPVT GAPQAPWAPA
     PVAEVVEAIE RDRPEVVFAA HVETAAGILL PDDYVRAIAD ATHAVGGVFI LDCIASGALW
     VDMADLHVDV LLSAPQKGWS GSPCAGFVML SETGRDRVMA TTSTSFAVDL QKWLTITEAY
     TEGQTPYHAT LPTDSLARDA ALMVETRALG LDVLRDAQTS LGARVRALLA ERGFPSVAAE
     GFAAPSVVVS FTDDPEIRTG AKFKRAGMQV AAGVPLMCGE RDDFSTFRLG LFGLDKLTDV
     DGTVERLAAH LKH
//