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
//