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Database: UniProt
Entry: D6Y9W7_THEBD
LinkDB: D6Y9W7_THEBD
Original site: D6Y9W7_THEBD 
ID   D6Y9W7_THEBD            Unreviewed;       511 AA.
AC   D6Y9W7;
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=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ADG90148.1};
GN   OrderedLocusNames=Tbis_3459 {ECO:0000313|EMBL:ADG90148.1};
OS   Thermobispora bispora (strain ATCC 19993 / DSM 43833 / CBS 139.67 / JCM
OS   10125 / KCTC 9307 / NBRC 14880 / R51).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Thermobispora.
OX   NCBI_TaxID=469371 {ECO:0000313|EMBL:ADG90148.1, ECO:0000313|Proteomes:UP000006640};
RN   [1] {ECO:0000313|EMBL:ADG90148.1, ECO:0000313|Proteomes:UP000006640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / KCTC 9307 /
RC   NBRC 14880 / R51 {ECO:0000313|Proteomes:UP000006640};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA   Wu D., Jando M., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Thermobispora bispora DSM 43833.";
RL   Submitted (JAN-2010) 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}.
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DR   EMBL; CP001874; ADG90148.1; -; Genomic_DNA.
DR   RefSeq; WP_013133681.1; NC_014165.1.
DR   AlphaFoldDB; D6Y9W7; -.
DR   STRING; 469371.Tbis_3459; -.
DR   KEGG; tbi:Tbis_3459; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_0_4_11; -.
DR   OrthoDB; 3335676at2; -.
DR   Proteomes; UP000006640; 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   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:UP000006640}.
FT   MOD_RES         321
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   511 AA;  55958 MW;  2C7EB03434E896D4 CRC64;
     MTSHGQTAPA DAVPEDARAH LFNDRNLDRY RRAVTEGVER VARRVARADR PFTGVSPARL
     AERISGIDLD RPLHDPTAAL DELDEVYLRD AVYFHHPRYL AHLNCPVVIP ALLGEAILSA
     INSSLDTWDQ SAGGTLIERR LIEWAAGRVG LGSDADGVFT SGGTQSNLQA LLLAREEACA
     KAMAGSPSLP RHEILRRLRV IASADGHFSV TKSARLLGLE PGAVILVETD ERRRMRPDAL
     ARELDRCRRD GLQVMAVVAT AGTTDFGAID PLPEIADLCG HADVWLHVDA AYGCGLLVSK
     TRRHLLNGIE RADSVTIDFH KSFFQPVSSS AVLVRDAATL RHATYHADYL NPAYAAEQRI
     PNQVDKSLQT TRRFDALKLW LTLRIMGPDA IGELFDRVVD RAAQAWELIN ADPRFEVLAK
     SQLSTVVFRY LPPEGPARKL TDDANLHARQ ALAASGQAMV AGTKVDGRHY LKLTLLNPET
     SLDDIAHVIG LLAGHAERYV TERSPLHCGT A
//
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