ID S2YTL8_9CORY Unreviewed; 462 AA.
AC S2YTL8;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Pyridoxal-dependent decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1219_02151 {ECO:0000313|EMBL:EPD67738.1};
OS Corynebacterium pyruviciproducens ATCC BAA-1742.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1125779 {ECO:0000313|EMBL:EPD67738.1, ECO:0000313|Proteomes:UP000014408};
RN [1] {ECO:0000313|EMBL:EPD67738.1, ECO:0000313|Proteomes:UP000014408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1742 {ECO:0000313|EMBL:EPD67738.1,
RC ECO:0000313|Proteomes:UP000014408};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Tong J., Walker B., Young S.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Corynebacterium pyruviciproducens 1773O (ATCC BAA-
RT 1742).";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPD67738.1}.
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DR EMBL; ATBY01000017; EPD67738.1; -; Genomic_DNA.
DR RefSeq; WP_016458887.1; NZ_KE150448.1.
DR AlphaFoldDB; S2YTL8; -.
DR STRING; 1125779.HMPREF1219_02151; -.
DR PATRIC; fig|1125779.3.peg.2096; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_011856_0_4_11; -.
DR Proteomes; UP000014408; Unassembled WGS sequence.
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:UP000014408}.
FT MOD_RES 291
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 462 AA; 50452 MW; FB2312FD8A6657BF CRC64;
MTSNPVTFNP RVPELATQFI GTIFNDYDPR SYAPGADFLT RQEDRQQVSP TAIPAVGRPL
AEATKELVDV LEHDSNLRHP RFFGFIPGPA QSVSWLGDVI ATAYNPHASN WAQSPGASAL
EKQVIDWACE AAGISAPNRG GILVSGGSMA NLTGLMAARE SRVPLDQIPR AVVYTTEQTH
SSVNKALRIL GISHIRTLPV DDAFRMQPTV LRQAIEADKK EGLLPFAVVG TCGTTNTGAI
DPLDAIADLC DEFDLWFHVD GAYGGSVVLS SRKADARGVE RCDSMAWDGH KWLFQTYGLA
MVLVKNRADL VRSFSAGGEY LQDVEGGSHN PDWWDMGPEL TRPARAPRLW LTLQTVGTER
LSQMIDSSIS VAELFEKEIQ SVEGISIVTP ACHAIVTFTT GDEAKNVALA EYLRRHNIAG
IWTTTLNGKN VLRLCTISPD ETEEDMEALV KDIEKALKKI QL
//
