ID C4R0D8_KOMPG Unreviewed; 497 AA.
AC C4R0D8;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=Glutamate decarboxylase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=PAS_chr2-1_0343 {ECO:0000313|EMBL:CAY68962.1};
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY68962.1, ECO:0000313|Proteomes:UP000000314};
RN [1] {ECO:0000313|EMBL:CAY68962.1, ECO:0000313|Proteomes:UP000000314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(2009).
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|RuleBase:RU000382}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FN392320; CAY68962.1; -; Genomic_DNA.
DR RefSeq; XP_002491242.1; XM_002491197.1.
DR AlphaFoldDB; C4R0D8; -.
DR SMR; C4R0D8; -.
DR STRING; 644223.C4R0D8; -.
DR EnsemblFungi; CAY68962; CAY68962; PAS_chr2-1_0343.
DR GeneID; 8199031; -.
DR KEGG; ppa:PAS_chr2-1_0343; -.
DR eggNOG; KOG0629; Eukaryota.
DR HOGENOM; CLU_011856_0_0_1; -.
DR InParanoid; C4R0D8; -.
DR OMA; RHATYHA; -.
DR OrthoDB; 888358at2759; -.
DR Proteomes; UP000000314; Chromosome 2.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.170; -; 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 PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 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:UP000000314}.
FT MOD_RES 307
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 497 AA; 55444 MW; 4F807AD9843B4F1C CRC64;
MTPIKTDLEA DRVTELETLL RPAVELIAQH IKDTDENDKP IGPYYPNPRD LYQSLKLEAD
FNGGGKDDEL VIQTVKKVLD SSVNTWNAGF MDKLYASTNV IGLVSDLLLS ALNTNSHVFT
VSPAVTIIEK YTARQYAGLF GFLGPRAGGL TFPGGSWSNV TSLQMARSSL YPDTKVKGNG
NHHFAVFASS HSHYSVEKAC ILLGIGAENL FKCKVDKNGC MDVTDLRVNI EKSIAEGYTP
LYINATAGTT VFGSYDSFED IHKIAKEYKC WFHIDGSWGG NVIFSDREKH KMKGSHLADS
ITANPHKMLG VPCTCSFLLV PDVSIFQQAN SLNAPYLFHN KHEDDDENYD LADGTMGCGR
RADSLKFYLS WLYYGSEGYK ERVDHAFSIA RYFTSKIVNR KGFKLVGSPE PACLQVCFYY
NPKNDFENGS ENTNATRYIA TELHKHGKFL VDYSPNPDDV DNQHGEFFRV VFNSPILDDK
TIDSLIDLIE QTGEEIV
//
