ID C5C3S3_BEUC1 Unreviewed; 455 AA.
AC C5C3S3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ACQ81982.1};
GN OrderedLocusNames=Bcav_3740 {ECO:0000313|EMBL:ACQ81982.1};
OS Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Beutenbergiaceae;
OC Beutenbergia.
OX NCBI_TaxID=471853 {ECO:0000313|EMBL:ACQ81982.1, ECO:0000313|Proteomes:UP000007962};
RN [1] {ECO:0000313|EMBL:ACQ81982.1, ECO:0000313|Proteomes:UP000007962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-8 / DSM 12333 / NBRC 16432
RC {ECO:0000313|Proteomes:UP000007962};
RX PubMed=21304633; DOI=10.4056/sigs.1162;
RA Land M., Pukall R., Abt B., Goker M., Rohde M., Glavina Del Rio T.,
RA Tice H., Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J., Jefferies C.C.,
RA Saunders E., Brettin T., Detter J.C., Han C., Chain P., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Beutenbergia cavernae type strain (HKI
RT 0122).";
RL Stand. Genomic Sci. 1:21-28(2009).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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DR EMBL; CP001618; ACQ81982.1; -; Genomic_DNA.
DR RefSeq; WP_015884219.1; NC_012669.1.
DR AlphaFoldDB; C5C3S3; -.
DR STRING; 471853.Bcav_3740; -.
DR KEGG; bcv:Bcav_3740; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_011856_0_4_11; -.
DR OrthoDB; 3335676at2; -.
DR Proteomes; UP000007962; Chromosome.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 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:UP000007962}.
FT REGION 28..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 291
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 455 AA; 47918 MW; CDB0B5B9B05D8EFB CRC64;
MDARERALSR AHDHAVDWLA SLGSRRVPPR ATTDEVATAL GRDLPDGPTD PADVVDLLAA
ASDPGLTAMP SGRFYGMVIG GTHPAALAAD WLVSAWDQNA ALNAVTPAAA AAEQVATAWL
LDLLGLPGDA AVGLATGATM ANFTCLAAAR DAVLRRHGWD QVTRGLTGAP RIRVLVGAER
HDSIDLVLRY LGLGTPHAVA VDDQGRIRPD ALAAALGDGP ADGPAIVALQ AGNVHSGAFD
PFDDAASLAH ERGAWVHVDG AFGLFAAASP RLRHLTRGLA DADSWATDAH KTLNVPYDCG
LAIVRDRSAL TTAMSMHGDY LIQDAAGDPF DTVPELSRRS RAVPVWAVLR SLGRRGVAEL
VERMADHAQA FAEGVAAIDG AEVLNDVVFT QVCASFGSDE RTREVVRRVL DDGTAWMSGS
RWRDRAVLRI SVCNWSTTDD DVGRSLDALR RAAAG
//
