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Database: UniProt
Entry: A0A132PPQ8_9MYCO
LinkDB: A0A132PPQ8_9MYCO
Original site: A0A132PPQ8_9MYCO 
ID   A0A132PPQ8_9MYCO        Unreviewed;       431 AA.
AC   A0A132PPQ8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Aminotransferase class III {ECO:0000313|EMBL:KWX24022.1};
GN   ORFNames=AFM11_11700 {ECO:0000313|EMBL:KWX24022.1};
OS   Mycolicibacterium wolinskyi.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=59750 {ECO:0000313|EMBL:KWX24022.1, ECO:0000313|Proteomes:UP000070612};
RN   [1] {ECO:0000313|EMBL:KWX24022.1, ECO:0000313|Proteomes:UP000070612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC_01 {ECO:0000313|EMBL:KWX24022.1,
RC   ECO:0000313|Proteomes:UP000070612};
RA   de Man T.J., Perry K.A., Coulliette A.D., Jensen B., Toney N.C.,
RA   Limbago B.M., Noble-Wang J.;
RT   "A draft genome sequence of Mycobacterium wolinskyi.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       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:KWX24022.1}.
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DR   EMBL; LGTW01000006; KWX24022.1; -; Genomic_DNA.
DR   RefSeq; WP_067848378.1; NZ_LGTW01000006.1.
DR   AlphaFoldDB; A0A132PPQ8; -.
DR   STRING; 59750.AWC31_30325; -.
DR   PATRIC; fig|59750.3.peg.6417; -.
DR   Proteomes; UP000070612; 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; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, 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:0000313|EMBL:KWX24022.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070612};
KW   Transferase {ECO:0000313|EMBL:KWX24022.1}.
SQ   SEQUENCE   431 AA;  44136 MW;  31282AB04788E152 CRC64;
     MNTLYERDEA VIAGIEKLRF FPLEVVSGHG CTLITPDGRE LLDLSATWTA SGLGHGHPAV
     ADAVSRAVRT APGAGGLSAV HPDSVGLAED LLALVPGTGE RRVYLGHAGS DANGVALRAC
     RHATGRRTVL AFEHSYHGGV GVAMGVSGVH VDAGVPADAD VAFLPYPNPF RPARDEVGAD
     VAACLDLANR HMATGTVACL IVEPILSDGG LVVPPDGFLA DLHEVCRLHG VPMICDEVKM
     GLGRPGTLHA FEHDGVVPDI VTFGKVLGGG LPLSSAVGPA ALLDEPAASA LLTTAGNPVC
     TAAGRAVLAT IVGEQLAERA AKVGAVLQDA LRALDSDVIG DVRGRGLAIG LELIDPATGG
     PDPRLAAQVS YRAWELGVVV YYVGGNVLEI TPPLILSEEQ AVRAADILGS AIDDAAAGKV
     DAEEVARYAG W
//
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