ID A0A2N3XUW0_SACSN Unreviewed; 374 AA.
AC A0A2N3XUW0;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=A8926_2055 {ECO:0000313|EMBL:PKW14439.1};
OS Saccharopolyspora spinosa.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=60894 {ECO:0000313|EMBL:PKW14439.1, ECO:0000313|Proteomes:UP000233786};
RN [1] {ECO:0000313|EMBL:PKW14439.1, ECO:0000313|Proteomes:UP000233786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44228 {ECO:0000313|EMBL:PKW14439.1,
RC ECO:0000313|Proteomes:UP000233786};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 Actinobacteria strains.";
RL Submitted (DEC-2017) 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|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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:PKW14439.1}.
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DR EMBL; PJNB01000001; PKW14439.1; -; Genomic_DNA.
DR RefSeq; WP_010694169.1; NZ_PJNB01000001.1.
DR AlphaFoldDB; A0A2N3XUW0; -.
DR STRING; 994479.GCA_000194155_02024; -.
DR OrthoDB; 9813612at2; -.
DR Proteomes; UP000233786; 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:InterPro.
DR CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR019880; OxyQ.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR03539; DapC_actino; 1.
DR PANTHER; PTHR42832; AMINO ACID AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42832:SF3; LL-DIAMINOPIMELATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:PKW14439.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000481}.
FT DOMAIN 41..372
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 374 AA; 39242 MW; FE785C46BC2CD30E CRC64;
MSSGTGPGAP APGPRGPQLP DFPWDSLAAQ TATARLHPDG IVNLSVGTPV DPVPENLQRA
LSAVADQPGY PATHGTPELR EAAVAALHRR HGVSGLVPDA VMPTIGSKEL VAWLPLLLGV
RPGDIVAIPD LAYPTYEVGA KIAGAEVVRL APGELPPPGT VLLWLNSPSN PTGRVLGAQQ
LADLVRAARE LGAVVAADEC YLALGWEAEP VSVLHPSVSS DFRGVLAVHS LSKSSNLAGY
RAGFITGDPD LVARVLELRK HAGMIVPRPV QEAITAALSD DAHVSAQREL YAARRAVLRP
ALEAAGFRIE HSEAGLYLWA TRGDGAWETV DWLARRGILV APGTFYGPAG DRHVRIALTA
TDERIAAVAK RLGE
//
