ID A0A101UVF1_9ACTN Unreviewed; 600 AA.
AC A0A101UVF1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=2,4-diaminobutyrate 4-aminotransferase {ECO:0000313|EMBL:KUO17545.1};
GN ORFNames=AQJ91_29540 {ECO:0000313|EMBL:KUO17545.1};
OS Streptomyces dysideae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=909626 {ECO:0000313|EMBL:KUO17545.1, ECO:0000313|Proteomes:UP000053260};
RN [1] {ECO:0000313|EMBL:KUO17545.1, ECO:0000313|Proteomes:UP000053260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RV15 {ECO:0000313|EMBL:KUO17545.1,
RC ECO:0000313|Proteomes:UP000053260};
RA Ruckert C., Abdelmohsen U.R., Winkler A., Hentschel U., Kalinowski J.,
RA Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces sp. RV15, isolated from a marine
RT sponge.";
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 -!- 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:KUO17545.1}.
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; LMXB01000074; KUO17545.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101UVF1; -.
DR STRING; 909626.AQJ91_29540; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000053260; 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; 2.
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; 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 SUPFAM; SSF53383; PLP-dependent transferases; 2.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 4: Predicted;
KW Aminotransferase {ECO:0000313|EMBL:KUO17545.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000053260};
KW Transferase {ECO:0000313|EMBL:KUO17545.1}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 600 AA; 61005 MW; 4A96E008E9FD739A CRC64;
MTVTESVRGG MPEPAGASAG ARAVQEGILR RQSARESAAR TYARALPIVP VRARGLTIEG
ADGRRYLDCL SGAGTLALGH NHPVVLEAIR KVLDSGAPLH VLDLATPVKD AFVTELFGTL
PPGLADHARV QFCGPAGTDA VEAAFKLVRA ATGRTGMLAF TGAYHGMTAG ALEASGGACD
VRVARLPYPR DYRCPFGVGG ERGAELAARW TESVLDDPKS GVPSPAGMIL EPVQGEGGVI
PAPDAWMRRM RQITADRNIP LIADEVQTGV GRTGAFWAVG HSGVTPDVMV LSKAIGGSLP
LAVVVYRDDL DAWEPGAHAG TFRGNQLAMA AGTATLAYVR ENGLAGRAAE LGARMLDQLQ
GLATEFACIG DVRGRGLMVG LEVVDPEASG GSVWGDGPVA GAWAESEGGG SRARASGRSA
GGGGWGQASA GPDGDRGRVG TPAGLDDGGD CAHASAGPDG DRGRIGTTAG SDGGWGWASA
GVGLDQAGGG PDLAAGLGSA GDGVGSAWVP DAARCPRPAA PELAAAIQRE CLRRGLIVEL
GGRHSSVVRL LPPLTISDEQ AAAVLDRLAD AVAAVARGRT APDQSHQPHP WHGDHAERAV
//
