ID   A0A1V2RDK1_9ACTN        Unreviewed;       503 AA.
AC   A0A1V2RDK1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=L-2,4-diaminobutyrate decarboxylase {ECO:0000313|EMBL:ONK10458.1};
DE            EC=4.1.1.86 {ECO:0000313|EMBL:ONK10458.1};
GN   ORFNames=STBA_11800 {ECO:0000313|EMBL:ONK10458.1};
OS   Streptomyces sp. MP131-18.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1857892 {ECO:0000313|EMBL:ONK10458.1, ECO:0000313|Proteomes:UP000189065};
RN   [1] {ECO:0000313|EMBL:ONK10458.1, ECO:0000313|Proteomes:UP000189065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP131-18 {ECO:0000313|EMBL:ONK10458.1,
RC   ECO:0000313|Proteomes:UP000189065};
RA   Paulus C., Rebets Y., Tokovenko B., Nadmid S., Terekhova L.P.,
RA   Myronovskyi M., Zotchev S.B., Rueckert C., Kalinowski J., Luzhetskyy A.;
RT   "New natural products identified by combined genomics-metabolomics
RT   profiling of marine Streptomyces sp. MP131-18.";
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:ONK10458.1}.
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DR   EMBL; LZNS01000001; ONK10458.1; -; Genomic_DNA.
DR   RefSeq; WP_077063124.1; NZ_LZNS01000001.1.
DR   AlphaFoldDB; A0A1V2RDK1; -.
DR   STRING; 1857892.STBA_11800; -.
DR   OrthoDB; 3335676at2; -.
DR   Proteomes; UP000189065; 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   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 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; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 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:UP000189065}.
FT   MOD_RES         305
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   503 AA;  54754 MW;  1F6E5F7B1B9CB851 CRC64;
     MSDDIGPALP EDQFRRLAHE TAGIVADYLA GIREDPVFRV MPDMVRRRLK EQALDEHSVS
     APQLIQEIRE FVLPYPMGNG HPRFFGWINS APAPVGILAE MLVAAQNPSA DVGDIAALHV
     ETAVLGWFKH LMGFPAEAAG ILVSGGTMAT MTGLAAARQW VAETDGWDVR REGVRPPDGR
     RLLIYVSEET HSSVRKAVEL LGLGSSALRT VEVDGRYRMD PDSLLRRIEQ DAGPGERPFC
     VVATAGTVNS GAIDPLARIA DICGRHGLWL HVDGAYGAVA STHPLVAPSF EGIARADSLS
     IDPHKWLSVP VECGCALVRD GDLLRRTFAY VPPYLHTEEG MGIGGPDFAQ YGFQQTRGFR
     ALKLWAVLRH MGGRGMRELI GRHLALAREL AGLIDDAPDL RMAAPVTLSV VAFRYVPQGT
     ADDPEALDRL NRAIEVEVQN DGRVFLSTTR LRGRLVLRAC VLHYDTRAED LVELVDVVRE
     IGADLAAKSA SHQSRPSTEA EGT
//