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Database: UniProt
Entry: A0A1D2IKF1_9ACTN
LinkDB: A0A1D2IKF1_9ACTN
Original site: A0A1D2IKF1_9ACTN 
ID   A0A1D2IKF1_9ACTN        Unreviewed;       481 AA.
AC   A0A1D2IKF1;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=L-2,4-diaminobutyrate decarboxylase {ECO:0000313|EMBL:ODA74981.1};
DE            EC=4.1.1.86 {ECO:0000313|EMBL:ODA74981.1};
GN   Name=ddc_1 {ECO:0000313|EMBL:ODA74981.1};
GN   ORFNames=APS67_000689 {ECO:0000313|EMBL:ODA74981.1};
OS   Streptomyces sp. AVP053U2.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1737066 {ECO:0000313|EMBL:ODA74981.1, ECO:0000313|Proteomes:UP000054731};
RN   [1] {ECO:0000313|EMBL:ODA74981.1, ECO:0000313|Proteomes:UP000054731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AVP053U2 {ECO:0000313|EMBL:ODA74981.1,
RC   ECO:0000313|Proteomes:UP000054731};
RA   Olsen C.W., Carey S., Hinshaw L., Karasin A.I.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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:ODA74981.1}.
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DR   EMBL; LMTQ02000003; ODA74981.1; -; Genomic_DNA.
DR   RefSeq; WP_042171002.1; NZ_LMTQ02000003.1.
DR   AlphaFoldDB; A0A1D2IKF1; -.
DR   OrthoDB; 3335676at2; -.
DR   Proteomes; UP000054731; Unassembled WGS sequence.
DR   GO; GO:0033983; F:diaminobutyrate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR   CDD; cd06450; DOPA_deC_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 1.20.1650.10; PLP-dependent transferases; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010977; Aromatic_deC.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054731}.
FT   MOD_RES         293
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   481 AA;  52322 MW;  D88C6FFE395D97A5 CRC64;
     MRSHLLNDTT AEHYRRSVTE GVERVAAKLA TTERPFTGVT VDALAPAVER IDLDRPLHDT
     TAALDELEDV YLRDAIYFHH PRYLAHLNCP VVIPAVLGEA VLSAVNSSLD TWDQSAGGTL
     IERKLIDWTA ARIGLGAAAD GVFTSGGTQS NLQALLLARE EAKTRDLGKL RVFSSEVSHF
     SVQKSAKLLG LGPDAVVSIP VDHDKRMQTV ALARELARCA EDGQVPMAVV ATAGSTDFGS
     IDPLPEIAGL CAQYGVWMHV DAAYGCGLLA SLKHRDRIDG IEHADSVTVD YHKSFFQPVS
     SSAVLVRDGA TLRHATYHAE YLNPRRMVTE RIPNQVDKSL QTTRRFDALK LWMTLRVMGA
     DGIGRLFDEV CDLAQDGWRL LAADPRFDVV VEPSLSTLVF RYVPAAVTDP SSIDRANLYA
     RKALFASGDA VVAGTKVAGR HYLKFTLLNP ETTTADITAV LDLIAGHAEQ YLGESLDRVA
     S
//
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