ID D7BU07_STRBB Unreviewed; 524 AA.
AC D7BU07;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=L-2,4-diaminobutyrate decarboxylase {ECO:0000313|EMBL:ADI09576.1};
GN OrderedLocusNames=SBI_06456 {ECO:0000313|EMBL:ADI09576.1};
OS Streptomyces bingchenggensis (strain BCW-1).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI09576.1, ECO:0000313|Proteomes:UP000000377};
RN [1] {ECO:0000313|EMBL:ADI09576.1, ECO:0000313|Proteomes:UP000000377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI09576.1,
RC ECO:0000313|Proteomes:UP000000377};
RX PubMed=20581206; DOI=10.1128/JB.00596-10;
RA Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA Xiang W.S.;
RT "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT bingchenggensis.";
RL J. Bacteriol. 192:4526-4527(2010).
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}.
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DR EMBL; CP002047; ADI09576.1; -; Genomic_DNA.
DR RefSeq; WP_014179027.1; NC_016582.1.
DR AlphaFoldDB; D7BU07; -.
DR STRING; 749414.SBI_06456; -.
DR KEGG; sbh:SBI_06456; -.
DR PATRIC; fig|749414.3.peg.6648; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_011856_0_4_11; -.
DR Proteomes; UP000000377; Chromosome.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
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; 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:UP000000377}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 330
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 524 AA; 56315 MW; 42CB1066C02B4CF3 CRC64;
MSLLAHPAED PSSGPIPGAA DGRAHLFNDR TADRYRRSVS DGVGLVASTV ARTTRPFTGV
TPAELAPEIA GIDLERPLGD PAAALDELER VYLKDAVYFH HPRYLAHLNC PVVIPALLGE
AILSAVNSSL DTWDQSAGGT LIERRLIDWT AARLGLGEAA DGIFTSGGTQ SNLHAMLLAR
DEACKLVEKE TAAAGAPLTK PQILPRLRIL ASQASHFSIA KAAAVLGLGY EAVIAVPCDQ
DRRMRTVALA RELDRCRRDG LVVMAVVATA GTTDFGSIDP LPEIADLCAR AGAWLHVDAA
YGCGLLVSPR RRHLLDGIER ADSVTVDYHK SFFQPVSSSA VLVRDRTTLS HATYHADYLN
PAHSAERLIP NQVDKSLQTT RRFDALKLWL TLRVMGADAV GELFDEVVDR AAEAWRLLDA
DPRYEVVTRP QLSTLVFRYT GGSADPGVLD RANLHAREAL AASGEAVVAG TVVDGAHYLK
FTLLNPETSV GDIAHVLDLI ACHADQYLSS PDAAEPEFTR ARAS
//
