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Database: UniProt
Entry: L8EVF5_STRR1
LinkDB: L8EVF5_STRR1
Original site: L8EVF5_STRR1 
ID   L8EVF5_STRR1            Unreviewed;       429 AA.
AC   L8EVF5;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Aspartate aminotransferase family protein {ECO:0000313|EMBL:QST84982.1};
GN   ORFNames=SRIM_036830 {ECO:0000313|EMBL:QST84982.1};
OS   Streptomyces rimosus subsp. rimosus (strain ATCC 10970 / DSM 40260 / JCM
OS   4667 / NRRL 2234).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1265868 {ECO:0000313|EMBL:QST84982.1, ECO:0000313|Proteomes:UP000011074};
RN   [1] {ECO:0000313|EMBL:QST84982.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 10970 {ECO:0000313|EMBL:QST84982.1};
RA   Pethick F.E., MacFadyen A.C., Tang Z., Sangal V., Tze-Tze L., Chu J.,
RA   Guo M., Kirby R., Hoskisson P.A., Herron P.R., Hunter I.S.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QST84982.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 10970 {ECO:0000313|EMBL:QST84982.1};
RA   Algora L., Schniete J.K., MacFadyen A., Hoskisson P.A., Hunter I.S.,
RA   Herron P.R.;
RL   Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:QST84982.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 10970 {ECO:0000313|EMBL:QST84982.1};
RA   Algora-Gallardo L., Schniete J.K., Mark D.R., Hunter I.S., Herron P.R.;
RT   "Bilateral symmetry of linear streptomycete chromosomes.";
RL   bioRxiv 0:0-0(2021).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP048261; QST84982.1; -; Genomic_DNA.
DR   RefSeq; WP_003980801.1; NZ_CP048261.1.
DR   AlphaFoldDB; L8EVF5; -.
DR   GeneID; 66859668; -.
DR   Proteomes; UP000011074; Chromosome.
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; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR049691; Daptide_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; NF041821; daptide_amino; 1.
DR   PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 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:QST84982.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:QST84982.1}.
SQ   SEQUENCE   429 AA;  45258 MW;  8CC7571EA7BCF271 CRC64;
     MTSGRHALWP SLLAPDQHGR DDLCAVSAEG VRVRFADGRE LLCGTSGLWN TNLGYGNQTI
     ADAAAEALRT ASYLSVFRYE NEYARRAADA LVELAGADHY VRVLFSTSGG AANDLAIKLA
     RQYQALRGMG GRKVVVGLRG SYHGLTFGGF ALTGEDLGQQ VYGVDQRLVR HVTPNEPGEL
     ATLMARQGAQ VAAVVVEPVL GSGAVPLSEE YIAELLRLRE EHGFLLVADE VATGFGRTGD
     FFASQRWPAR PDLLITSKGL TNGTSAAAAV LAAQLVADVF DDTGVVLSHG ETQAGTPVTC
     ATILATISEM HRLDAVALGR RLAGRLEEEL GTLVAEHPLV NGTTGVGCFR SVRVTAADRS
     GAPLPQPEVP SLVSAVREAG ALVHPGLHGI QLFPALTYTD TELDELLACI RAGLGLYADR
     VAARAEARG
//
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