ID   A0A0K1ELB8_CHOCO        Unreviewed;       761 AA.
AC   A0A0K1ELB8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Decarboxylase {ECO:0000313|EMBL:AKT41408.1};
GN   ORFNames=CMC5_056080 {ECO:0000313|EMBL:AKT41408.1};
OS   Chondromyces crocatus.
OC   Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae;
OC   Chondromyces.
OX   NCBI_TaxID=52 {ECO:0000313|EMBL:AKT41408.1, ECO:0000313|Proteomes:UP000067626};
RN   [1] {ECO:0000313|EMBL:AKT41408.1, ECO:0000313|Proteomes:UP000067626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cm c5 {ECO:0000313|EMBL:AKT41408.1,
RC   ECO:0000313|Proteomes:UP000067626};
RA   Zaburannyi N., Bunk B., Maier J., Overmann J., Mueller R.;
RT   "Genome analysis of myxobacterium Chondromyces crocatus Cm c5 reveals a
RT   high potential for natural compound synthesis and the genetic basis for the
RT   loss of fruiting body formation.";
RL   Submitted (JUL-2015) 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};
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DR   EMBL; CP012159; AKT41408.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K1ELB8; -.
DR   STRING; 52.CMC5_056080; -.
DR   KEGG; ccro:CMC5_056080; -.
DR   PATRIC; fig|52.7.peg.6180; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000067626; 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; 3.40.640.10; 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   PANTHER; PTHR42735; -; 1.
DR   PANTHER; PTHR42735:SF4; TYROSINE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067626}.
FT   MOD_RES         479
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   761 AA;  84441 MW;  DE8ABB7DF258A70D CRC64;
     MSGGEAPLME RGVLAMDEGD ALMLTRVHKK PGFVTVRRHG PRTVNVGKYS SVPDIGAAPI
     DEPAAWFLGP RAENSEVLTT LTKDVLEHIG AYRRGYLPED PIIITPEMQA TSSYTTAVAE
     MSTSFKEVLG YFAERATPFF SLRYQAHMTG DNPMPALAGY FLGMLHNPNN VTIQASTTTT
     LLELLAMRDL CHMVGWSTEN DDQAWSHITA DGSIANNEAV WTAREVKFLP FAIVKALQKE
     PSLAGAKDVE VTLTSGTKKR LDQTTNWERF NIRRDEILAL PGRMAAKLGK QPYEVWSVVV
     NYDVNAVGVW GMLDAFEGLG GAPTLFTPST RHYSWPKAAA VNGFGTERDV TMMVDADGRM
     SIDELTKGLD TALSKKIPVL LVVAVNGSTE ESAIDDLTKI LAVREDYRKK GLEFDIHVDA
     AWGGYFMTVV RKDFGSVVTP ADLENPFIED TRKVPMSDYS IEQFKAVREV DSVTIDPHKS
     GYIQYTAGSI LYRNKEVLNL VTFTGAYIGA ATEPTVGMFG LEGSKAGATA ASVFFAHRCI
     RPSERGYGRI LTFALQNTRR LYTDLLFLSR PEDSFVCTPL PRIPAERSGA SAAEQEKQLA
     FIKETIWGKT IEEIEANPEA LALFRELGPD QNILDYGFNP RVDGKVNTDP EAYNQLMQGV
     YDAFHIHYDK EGLADNIHNY KLLLSYTIFK RHEYGDAFMD TFAKRLGLEG RPEELYCLRS
     VIMDPYALNL NSAFTQQLVD ILRDKVNELA RRTSRSASPS A
//