ID U4UTD4_DENPD Unreviewed; 549 AA.
AC U4UTD4;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Glutamate decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=D910_10672 {ECO:0000313|EMBL:ERL93380.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL93380.1, ECO:0000313|Proteomes:UP000030742};
RN [1] {ECO:0000313|EMBL:ERL93380.1, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
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; KB632355; ERL93380.1; -; Genomic_DNA.
DR AlphaFoldDB; U4UTD4; -.
DR STRING; 77166.U4UTD4; -.
DR OrthoDB; 888358at2759; -.
DR Proteomes; UP000030742; Unassembled WGS sequence.
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 CDD; cd06450; DOPA_deC_like; 1.
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:SF12; BLACK, ISOFORM A; 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:UP000030742}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 352
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 549 AA; 62207 MW; D8121E6B50DC76D3 CRC64;
MPANGQGEIN VDESESYSDT LASSEDEEAA CLSRTIERSF TTTTLPADKL ATIESLPSKR
DHEAFFRECI DIMLREAIFE GTSRRTKVLD FKQPETLLKL LDFDLKAQPS SHSDLIKSLK
DVIKYSVKTG HPYFVNQLFS SVDPYGFVGQ MLTDALNPSA YTYEVAPVVI LMEETVLREM
RQIVGWPNGE GDGIFCPGGS MANGYAISCA RHYYFPEVKT KGLHGLPKLV LFTSEDAHYS
IKKLASFLGL GTENVHLVNT NSQGKMDPDH LEQLINTSLE NGERPFMVSS TAGTTVIGAF
DPIEKLADIC KKNNMWLHVD AAWGGGALIS KKHRNLLKGI ERADSVTWNP HKLLTAPQQC
STLLVKHKNV LSEAHSANAA YLFQKDKFYD TQYDTGDKHI QCGRKADVLK FWFMWKAKGT
SGLEQHIDKV FENAQYFYEN IKQRPGFQIV IPEPECTNIC FWYVPESLRM NSTEEFLDKL
QNDGEYKEKL HRVAPKIKEK MMTEGTMMVT YQTYKEKPNF FRMVFQSSGL DKNDMLHLIQ
EFERLGQGL
//
