ID F3ZJN7_9ACTN Unreviewed; 387 AA.
AC F3ZJN7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Putative 2,4-diaminobutyrate 4-transaminase {ECO:0000313|EMBL:EGJ74322.1};
GN ORFNames=STTU_1534 {ECO:0000313|EMBL:EGJ74322.1};
OS Streptomyces sp. Tu6071.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=355249 {ECO:0000313|EMBL:EGJ74322.1};
RN [1] {ECO:0000313|EMBL:EGJ74322.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tu6071 {ECO:0000313|EMBL:EGJ74322.1};
RA Erxleben A., Wunsch-Palasis J., Gruening B.A., Luzhetska M., Bechthold A.,
RA Gunther S.;
RT "Genome sequence of Streptomyces sp. Tu6071.";
RL Submitted (APR-2011) 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}.
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DR EMBL; CM001165; EGJ74322.1; -; Genomic_DNA.
DR AlphaFoldDB; F3ZJN7; -.
DR HOGENOM; CLU_016922_10_0_11; -.
DR Proteomes; UP000003955; Chromosome.
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: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; 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 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; 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 387 AA; 40821 MW; 929CB5818C4D0AC6 CRC64;
MVLQAIRDVL DSEAPLHVLD LATPVKDAFV TELFRTLPGE LAARGRIQFC GPAGTDAVEA
ALKLVRRATG RQAVLGFTGA YHGMTAGALD VSSAATSVRD TLRLPYPQDY RCPFGVGGEE
GAALGARLAE SYLDDPKSGV PEPAGMIVEP VQGEGGVHPA PDAWLRRMRA LTRARGLPLI
ADEVQTGVGR TGAFWAVDHA GVVPDVMVLS KAIGGSLPLA VIVYHEDLDV WEPGAHAGTF
RGNQLAMAAG AATLAHVREN GLAERARLLG ARMLSALRSL ATRHAWIGDV RGRGLMLGVE
LVDPEAARPG SDGPPPADAA RAVAVRRECL RRGLIVELGG RHSAVVRLLP PLTLTDDQAT
AVLDRFADAL DAVDRDPRVR APRTPPV
//