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
//