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Database: UniProt
Entry: A0A1Q5KVL1_9ACTN
LinkDB: A0A1Q5KVL1_9ACTN
Original site: A0A1Q5KVL1_9ACTN 
ID   A0A1Q5KVL1_9ACTN        Unreviewed;       454 AA.
AC   A0A1Q5KVL1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Aspartate aminotransferase family protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AMK31_15855 {ECO:0000313|EMBL:OKJ85556.1};
OS   Streptomyces sp. TSRI0107.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703942 {ECO:0000313|EMBL:OKJ85556.1, ECO:0000313|Proteomes:UP000185813};
RN   [1] {ECO:0000313|EMBL:OKJ85556.1, ECO:0000313|Proteomes:UP000185813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSRI0107 {ECO:0000313|EMBL:OKJ85556.1,
RC   ECO:0000313|Proteomes:UP000185813};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKJ85556.1}.
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DR   EMBL; LIVZ01000005; OKJ85556.1; -; Genomic_DNA.
DR   RefSeq; WP_073941192.1; NZ_LIVZ01000005.1.
DR   AlphaFoldDB; A0A1Q5KVL1; -.
DR   STRING; 1703942.AMK31_15855; -.
DR   OrthoDB; 9801834at2; -.
DR   Proteomes; UP000185813; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}.
SQ   SEQUENCE   454 AA;  50263 MW;  583B87F4FF448251 CRC64;
     MSTKDLSQSA YDHLWMHFTR MSSYENSPVP TIVRGEGTYI YDDKGKRYLD GLAGLFVVQA
     GHGRTELAET AFKQAQELAF FPVWSYAHPK AVELAERLAD YAPGDLNKVF FTTGGGEAVE
     TAWKLAKQYF KLQGKPTKYK VISRAVAYHG TPQGALSITG LPGLKAPFEP LVPGAHKVPN
     TNIYRAPIFG DDPEAFGRWA ADQIEQQILF EGPETVAAVF LEPVQNAGGC FPPPPGYFQR
     VREICDKYDV LLVSDEVICA FGRLGTIFAC DKFGYVPDMI TCAKGMTSGY SPIGACIVSD
     RIAEPFYKGD NTFLHGYTFG GHPVSAAVGL ANLDLFEREN LTQHVLDNEG AFLQTLQKLH
     DLPIVGDVRG NGFFYGIELV KDKNTKESFN EEETERVLYG FLSKALFDNG LYCRADDRGD
     PVIQLAPPLI SDQETFDEIE QILRATLTEA WTKL
//
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