ID   A0A176KWD5_9ACTN        Unreviewed;       461 AA.
AC   A0A176KWD5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:OAA96585.1};
GN   ORFNames=A6P39_32835 {ECO:0000313|EMBL:OAA96585.1};
OS   Streptomyces sp. FXJ1.172.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=710705 {ECO:0000313|EMBL:OAA96585.1};
RN   [1] {ECO:0000313|EMBL:OAA96585.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FXJ1.172 {ECO:0000313|EMBL:OAA96585.1};
RA   Liu M., Liu N., Shang F., Huang Y.;
RT   "Activation and identification of NC-1, a novel cryptic cyclodepsipeptide
RT   from red soil-derived Streptomyces sp. FXJ1.172.";
RL   Submitted (APR-2016) 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:OAA96585.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LWRP01000168; OAA96585.1; -; Genomic_DNA.
DR   RefSeq; WP_067053829.1; NZ_CP119133.1.
DR   AlphaFoldDB; A0A176KWD5; -.
DR   STRING; 710705.A6P39_32835; -.
DR   OrthoDB; 9801052at2; -.
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   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:OAA96585.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:OAA96585.1}.
SQ   SEQUENCE   461 AA;  50199 MW;  DC3EE70099488583 CRC64;
     MSTEFDLGTL LAERGAERYE LHTKYLNPQL ARMLHTIGFD KVYERAEGAH FFDADGNDYL
     DMLAGFGVMG LGRHHPVVRK ALHDVLDLDL ADLTRFDCQP LPGLLAERLL VHSPHLDRVF
     FGNSGTEAVE TALKFARYAT GKPRVLYCDH AFHGLTTGSL SVNGEDGFRD GFAPLLPDTA
     IPLGDLDALA RELKKGDVAA LIVEPIQGKG VHEAPPGYLR AAQDLLHRHK ALLIADEVQT
     GLGRTGDFYA YQHEDGVEPD LVCVAKALSG GYVPVGATLG KDWIFKKVYS SMDRVLVHSA
     SFGSGAQAMA CGLAVLSVME NEQIVAGVRT TGELLKSRLA ALIGKYELLA DVRGRGLMIG
     IEFGKPSSLK LRGRWTMLQA ARKGLFAQMV VVPLLQRHRI LTQVSGDHLE VIKLIPPLII
     DEADVDRFVD AFTAVMDDAH SGGGLMWDFG KTLIKQAVAG R
//