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Database: UniProt
Entry: A0A101SS78_9ACTN
LinkDB: A0A101SS78_9ACTN
Original site: A0A101SS78_9ACTN 
ID   A0A101SS78_9ACTN        Unreviewed;       457 AA.
AC   A0A101SS78;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=2,4-diaminobutyrate 4-aminotransferase {ECO:0000313|EMBL:KUN78964.1};
GN   ORFNames=AQJ66_30210 {ECO:0000313|EMBL:KUN78964.1};
OS   Streptomyces bungoensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=285568 {ECO:0000313|EMBL:KUN78964.1, ECO:0000313|Proteomes:UP000053024};
RN   [1] {ECO:0000313|EMBL:KUN78964.1, ECO:0000313|Proteomes:UP000053024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 41781 {ECO:0000313|EMBL:KUN78964.1,
RC   ECO:0000313|Proteomes:UP000053024};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces bungoensis DSM 41781, type strain
RT   for the species Streptomyces bungoensis.";
RL   Submitted (OCT-2015) 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:KUN78964.1}.
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DR   EMBL; LMWX01000056; KUN78964.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101SS78; -.
DR   STRING; 285568.AQJ66_30210; -.
DR   Proteomes; UP000053024; 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; 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; IPR004637; Dat.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00709; dat; 1.
DR   PANTHER; PTHR43552; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43552:SF1; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 4.
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:KUN78964.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053024};
KW   Transferase {ECO:0000313|EMBL:KUN78964.1}.
FT   REGION          339..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..449
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   457 AA;  47459 MW;  B80625B00056A13A CRC64;
     MPVRARGLTI EGADGRRYLD CLSGAGALAL GHNHPVVLEA VRRVLDSGAP LSVLDLATPV
     KDAFVTELFR TLPPGLADRA RIQFCGPAGT DAVEAAFTLV RAATGRTGLL AFTGAYHGMT
     AGALAASGGA GDVGVARLPY PQDYRCPFGI GGPVGAELAA RWTESLLDDP KSGVPLPAGM
     ILEPVQGEGG VLPAPDDWLR RMRTITADRS VPLIADEIQT GVGRTGAFWA VGHSGITPDV
     MVLSKAIGGS LPLAVVVYRD DLDVWQPGAH AGTFRGNQLA MAAGAATLAY VRENGLAERA
     AALGSRMLSR LRRLQTELPC VGDVRGRGLM IGVELVDPEG ENTGPGHGAP GASSAGVHGA
     IPSALEPVRA PRPADPELAA AVQRECLNRG LIVELGGRHA AVVRILPPLT ISDEQAAAVL
     DRLSDAIAAA ARHQQHHGRR RHHGQHHGPA PHIGRQP
//
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