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Database: UniProt
Entry: A0A0M8T4F8_9ACTN
LinkDB: A0A0M8T4F8_9ACTN
Original site: A0A0M8T4F8_9ACTN 
ID   A0A0M8T4F8_9ACTN        Unreviewed;       519 AA.
AC   A0A0M8T4F8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Class III aminotransferase {ECO:0000313|EMBL:KOU47993.1};
GN   ORFNames=ADK55_20065 {ECO:0000313|EMBL:KOU47993.1};
OS   Streptomyces sp. WM4235.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415551 {ECO:0000313|EMBL:KOU47993.1, ECO:0000313|Proteomes:UP000037699};
RN   [1] {ECO:0000313|EMBL:KOU47993.1, ECO:0000313|Proteomes:UP000037699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM4235 {ECO:0000313|EMBL:KOU47993.1,
RC   ECO:0000313|Proteomes:UP000037699};
RA   Noorani M.;
RL   Submitted (JUL-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:KOU47993.1}.
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DR   EMBL; LGDE01000293; KOU47993.1; -; Genomic_DNA.
DR   RefSeq; WP_053680603.1; NZ_LGDE01000293.1.
DR   AlphaFoldDB; A0A0M8T4F8; -.
DR   PATRIC; fig|1415551.3.peg.4374; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000037699; 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   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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11986:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:KOU47993.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037699};
KW   Transferase {ECO:0000313|EMBL:KOU47993.1}.
SQ   SEQUENCE   519 AA;  56535 MW;  18F6BABF157879AB CRC64;
     MTAEPTTATT EYAEPFLLGV LASGGLDAEY VRGEGNTLYL RDEDGREIPV LDYVGGYGSL
     MLGHNHPGIN AYAKELLDAQ TPVHAQFSRH PYANDVAEVL NRIIQRERGD DEQYYAIFAN
     SGAEAVEAAI KHAELDRGLR LTALSDEIAA HLADVRGQVE AGVASVPAAV AESFEDLVTD
     VLARNEAQRG RSPLFLVPEG GFHGKLAGSV QLTHNEGYRL PFKALAAQSR FVPRDRPGTI
     RKIIDEERAH LLDLVVEGGQ VQVVERDFPL FVAFVLEPVL GEGGIHELSR EFADEIQEVC
     AETGIPIVID EVQTGMGRTG SFLAATHLGL RGDYYTLAKS LGGGIAKAAV MLVRKPLYRG
     QFELAHSSTF AKDSFSCLIA LKVLELMEAD DGEVYRRAAE RGARLLAMLR SVRDDFPETV
     KDVRGRGLML GLEFHDQSGS SAEPLKAVAQ SGFFGYFVAG HMLRAHRIRT FPTSSAVNTL
     RFEPSVYLTD EEIGRLEEAL RDVCVIIRDT DGASLAPIA
//
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