ID A0A0Q8PTI9_9ACTN Unreviewed; 412 AA.
AC A0A0Q8PTI9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Aminotransferase V {ECO:0000313|EMBL:KRB76940.1};
GN ORFNames=ASE01_09220 {ECO:0000313|EMBL:KRB76940.1};
OS Nocardioides sp. Root190.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736488 {ECO:0000313|EMBL:KRB76940.1, ECO:0000313|Proteomes:UP000050886};
RN [1] {ECO:0000313|EMBL:KRB76940.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB76940.1,
RC ECO:0000313|Proteomes:UP000050886};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB76940.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB76940.1,
RC ECO:0000313|Proteomes:UP000050886};
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|PIRSR:PIRSR000524-50};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236}.
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:KRB76940.1}.
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DR EMBL; LMIA01000009; KRB76940.1; -; Genomic_DNA.
DR RefSeq; WP_056750577.1; NZ_LMIA01000009.1.
DR AlphaFoldDB; A0A0Q8PTI9; -.
DR STRING; 1736488.ASE01_09220; -.
DR Proteomes; UP000050886; 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 InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KRB76940.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000050886};
KW Transferase {ECO:0000313|EMBL:KRB76940.1}.
FT DOMAIN 42..213
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 367
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 412 AA; 43513 MW; E3FCB531CDE39BA6 CRC64;
MSHQEIAPPP RLLMGPGPIS ADPRVLRAMA APLVGQFDPF MTTTMNEVMG LYRTVFDTAN
EQTFLVDGTS RAGIEAALVS LVEPGDRVLV PVFGRFGHLL AEIAGRCGAE VHTIEVPWGQ
VFAPEAIEDA VRAVRPKVLA CVQGDTSTTM CQPLAEIGAI CREHDVLLYC DATASLGGNE
FRTDAWGIDI ATAGLQKCLG GPSGSAPITI SPRAVEMIGA RRHVEAGLRE IPGGEDVDAA
RGRVIASNYF DLAMVMDYWG PRRLNHHTEA TSMLYAARES ARLLVTEGVD TAVARHERHG
RAMLDGVRGL GLGVFGDVAH KMSNVVAVEI PEALGAAGGD AVRGSLLDDF GIEIGTSFGP
LHGKVWRIGT MGFNARKDAV LTTLAALEQV LRAHGVAVPP GGGVAAAQEV YA
//
