ID   A0A0B5HW45_9ACTN        Unreviewed;       455 AA.
AC   A0A0B5HW45;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Amino acid decarboxylase {ECO:0000313|EMBL:AJF64656.1};
GN   ORFNames=SVTN_09685 {ECO:0000313|EMBL:AJF64656.1};
OS   Streptomyces vietnamensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=362257 {ECO:0000313|EMBL:AJF64656.1, ECO:0000313|Proteomes:UP000031774};
RN   [1] {ECO:0000313|EMBL:AJF64656.1, ECO:0000313|Proteomes:UP000031774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GIMV4.0001 {ECO:0000313|Proteomes:UP000031774};
RA   Deng M.R., Guo J., Ma L.Y., Feng G.D., Mo C.Y., Zhu H.H.;
RT   "Complete genome sequence of Streptomyces vietnamensis strain GIMV4.0001, a
RT   genetic manipulable producer of the benzoisochromanequinone antibiotic
RT   granaticin.";
RL   Submitted (DEC-2014) 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|RuleBase:RU000382}.
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DR   EMBL; CP010407; AJF64656.1; -; Genomic_DNA.
DR   RefSeq; WP_041128710.1; NZ_CP010407.1.
DR   AlphaFoldDB; A0A0B5HW45; -.
DR   STRING; 362257.SVTN_09685; -.
DR   KEGG; svt:SVTN_09685; -.
DR   HOGENOM; CLU_011856_0_4_11; -.
DR   Proteomes; UP000031774; Chromosome.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.170; -; 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; 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   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:UP000031774}.
FT   MOD_RES         285
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   455 AA;  46833 MW;  571A1D27A5167044 CRC64;
     MRAAPPPLAV DPTALSRLLG IALDALREGA QARGGPFPAG GPGAVARRIA ALGAVLPETG
     TGPDEALRTL ARVLAEGAAD PAHPLCAAHL HTPPLALAAA ADLAASALNP SMDSWDQAPA
     ASALEAEVTA ALAAEVFPDA KTPDALVTTG GTESNQLALL LARERHGAGL RTVVGANAHH
     SFRRAAWLLG LPEPVVVPAP HGTMDPAALA EALDQDGPTL VAATAGTTDE GLIDPLPEIA
     DVCAAAGAEL HVDAAYGGPV LFSRTHRRLL DGLDRARTVT VDLHKLGWQP AAAGLLAVRD
     AADPAVLGHT ADYLNADDDT EAGLPDLLGR SLRTTRRPDV LKTAVTLRAL GRSGLGSLVD
     TCMELARDFA DLVEKAPGFD LHARPTLTTV LFRPTGAEDE TVAAIRRTLL AEGRAVLGRA
     TADGRLWLKA TLLNPHTTPA DLADILTLVE GSTHR
//