ID A0A0G3ABD6_9ACTN Unreviewed; 418 AA.
AC A0A0G3ABD6;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:AKJ09622.1};
GN ORFNames=ABB07_06200 {ECO:0000313|EMBL:AKJ09622.1};
OS Streptomyces incarnatus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=665007 {ECO:0000313|EMBL:AKJ09622.1, ECO:0000313|Proteomes:UP000035366};
RN [1] {ECO:0000313|EMBL:AKJ09622.1, ECO:0000313|Proteomes:UP000035366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL8089 {ECO:0000313|Proteomes:UP000035366};
RX PubMed=26159526;
RA Oshima K., Hattori M., Shimizu H., Fukuda K., Nemoto M., Inagaki K.,
RA Tamura T.;
RT "Draft Genome Sequence of Streptomyces incarnatus NRRL8089, which Produces
RT the Nucleoside Antibiotic Sinefungin.";
RL Genome Announc. 3:e00715-e00715(2015).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR EMBL; CP011497; AKJ09622.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3ABD6; -.
DR STRING; 665007.ABB07_06200; -.
DR PATRIC; fig|665007.5.peg.1357; -.
DR Proteomes; UP000035366; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:AKJ09622.1};
KW Hydrolase {ECO:0000313|EMBL:AKJ09622.1};
KW Protease {ECO:0000313|EMBL:AKJ09622.1}.
FT DOMAIN 34..320
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 418 AA; 43468 MW; B7C797E6EC1A360D CRC64;
MRRTDPEGHG PVRYGPPLPG DGLPVLPELT AVLAAAAGRA DAQPVGGAPA LLEAACGYWT
RRGLPTVPDQ VAAGPGAPAL LLALTAALAS DGGDVLVPRP CAAWWAPYAR VLGRPAYHVP
TPAESGGVPD PYAFLETVRR VRAEGGDPRL LVLSVADDPT ATVAPPELLH ETVEAATAEG
LHLVSDETWR DTLHHPHDTV LLSPAEMLPD RVTVVTDLAG SLLPPGWPAA VARFPATEPG
QHLHARVLDI LTGLGARVAA PVAAAAGYAL DEPPPVIERR EAAVRLHAGV AAAAHAAVVA
GGALARPPQA GRHLYADLGP LREPLAEQGV GDAQELEDLL TARLGMPAPG GHRFGDDLAA
LRVRLATGPL LGGSDEERAE CLTSPVPLEL PHVQRALISL TSVLDDLRDD AQRWEPPR
//
