ID   D7B1C5_NOCDD            Unreviewed;       551 AA.
AC   D7B1C5;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ADH66516.1};
GN   OrderedLocusNames=Ndas_1074 {ECO:0000313|EMBL:ADH66516.1};
OS   Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM
OS   7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509)
OS   (Actinomadura dassonvillei).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Nocardiopsis.
OX   NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH66516.1, ECO:0000313|Proteomes:UP000002219};
RN   [1] {ECO:0000313|EMBL:ADH66516.1, ECO:0000313|Proteomes:UP000002219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 /
RC   NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509
RC   {ECO:0000313|Proteomes:UP000002219};
RX   PubMed=21304737; DOI=10.4056/sigs.1363462;
RA   Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H., Cheng J.F.,
RA   Tapia R., Han C., Goodwin L., Pitluck S., Pagani I., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Djao O.D., Rohde M., Sikorski J.,
RA   Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Nocardiopsis dassonvillei type strain (IMRU
RT   509).";
RL   Stand. Genomic Sci. 3:325-336(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; CP002040; ADH66516.1; -; Genomic_DNA.
DR   RefSeq; WP_013152123.1; NC_014210.1.
DR   AlphaFoldDB; D7B1C5; -.
DR   STRING; 446468.Ndas_1074; -.
DR   KEGG; nda:Ndas_1074; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_0_4_11; -.
DR   OrthoDB; 3335676at2; -.
DR   Proteomes; UP000002219; Chromosome 1.
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   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:UP000002219}.
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         338
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   551 AA;  59663 MW;  3523DEBDAB01B340 CRC64;
     MSSLARSAPG PLHGNAGALG TRPTPPSGQD PDDPRTQLFD ARSAERYRDL TGEAAARVAR
     RIAGADRPLT GATAEDLRPQ IDKVDLDQPL HDPTAALDEL ERVYLDDAVY FHHPRYMGHL
     NCPVVLPALL GETVLSAVNS SLDTWDQSAG GTLIEQRLID WTCERVGFGE TADGVFTSGG
     SQSNLQALLM ARDEAHHRAK AQEGQDTRLA ELLPRMRVLT SEAGHFSVAK SAALLGLGYE
     SVITVACDDR RRMRPDALAA QLRRCRAEGL LPIAVVATAG TTDFGSIDPL PRIADLCRQR
     GVWMHVDAAY GCGLLVSRHR HLLEGVERAD SVTVDFHKSF FQPVSSSAIV VRDRDVLRHV
     TYHADYLNSR SDGSTPLLSP NQVDKSLQTT RRFDALKLWL TLRVMGADGV GALFDSVLDL
     AATAWTLLDA DPRFTVVTRP SLSTLVFRCA VPGADPDTAD AAHRYAREAL LASGRAFVAR
     TTVDGRPHLK LTLLNPRATR EDVAEVLDLI AAHVDHFMNG RDIPDRPAPP APTTTAAHAA
     SALPTTTGRS R
//