ID A0A0Q8PT38_9ACTN Unreviewed; 462 AA.
AC A0A0Q8PT38;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:KRB75233.1};
GN ORFNames=ASE03_14515 {ECO:0000313|EMBL:KRB75233.1};
OS Kitasatospora sp. Root187.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=1736486 {ECO:0000313|EMBL:KRB75233.1, ECO:0000313|Proteomes:UP000051829};
RN [1] {ECO:0000313|EMBL:KRB75233.1, ECO:0000313|Proteomes:UP000051829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root187 {ECO:0000313|EMBL:KRB75233.1,
RC ECO:0000313|Proteomes:UP000051829};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB75233.1, ECO:0000313|Proteomes:UP000051829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root187 {ECO:0000313|EMBL:KRB75233.1,
RC ECO:0000313|Proteomes:UP000051829};
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 -!- 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:KRB75233.1}.
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DR EMBL; LMHX01000003; KRB75233.1; -; Genomic_DNA.
DR RefSeq; WP_057236517.1; NZ_LMHX01000003.1.
DR AlphaFoldDB; A0A0Q8PT38; -.
DR STRING; 1736486.ASE03_14515; -.
DR Proteomes; UP000051829; 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:UniProt.
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; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF121; BLR3010 PROTEIN; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 3.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KRB75233.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000051829};
KW Transferase {ECO:0000313|EMBL:KRB75233.1}.
SQ SEQUENCE 462 AA; 50750 MW; B4A5A2C505AF47C9 CRC64;
MPADRLDLSA LLAERGAERY ELQAKYLNPQ LARMLHTIGF DKFYERAEGA YFYDAEGNDY
LDMLAGFGIF ALGRHHPVVR DAVRQVMDLD LPDLTRFDCA PLPGLLAEQL LAYTPGLDRV
FFGNSGTEAV ETALKFARYA TGRKRILYCD HAFHGLTTGS LSVNGENGFR KGFDPLLPDT
AVPLGDLGAL ARELRKGDVA ALIVEPIQGK GVLAPPPGWL LAAQQLLHEH KALLICDEVQ
TGIGRTGSFF AYQQEEGVLP DLVCAAKALS GGYVPIGATL GKGWIFEKVY SSMDRVLVHS
ASFGSNAQAM AAGLATLHVM REEKVVENAH RVGELFRSRL AGLVEKYELL AEVRGRGLMI
GIEFGRPKSL KLRTGWTALQ AARKGLFAQM VVVPLLQRHR ILTQVSGDHL EVIKLIPPLI
ITEREVDRFV DAFTDVMDDA HRGSGLMWDF GRTLVKQAVV KA
//
